Antibiotics For Research Applications - BioFiles Issue 4.3

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BioFiles
Volume 4, Number 3
Antibiotics for
Research Applications
Antimicrobial Peptides
Antifungals
New Antibiotics
Special Offer for Ready Made Solutions
Scribd Readers! Antibiotic Selector
See page 3 for

more details.
Peptides perturbing bacterial cell wall and

extracting liposomal sphere, resulting in cell death.
Life Science
BioFiles
Volume 4, Number 3
Your gateway to Biochemicals and Reagents

for Life Science Research from Sigma® Table of Contents
Introduction 3
Antimicrobial Peptides 4
Bacteriocins 5
Insect RAMPs 5
Mammalian RAMPs 6
Bacterial Cell Killing Mechanisms 7
Antifungals 10
Antifungal Mechanisms of Action 10
BioFiles Online allows you to: Drug Resistance by Fungi 11
• Access any issue of BioFiles Antifungals that Bind Ergosterol
• Subscribe for: or Inhibit Biosynthesis 12
✓ future issues Inhibits β-(1→3)Glucan Synthesis 13
✓ eBioFiles email notifications Chitin Synthesis Inhibitors 13
• Stay up-to-date on the latest BioNews from Sigma Interferes with DNA, RNA, or Protein Synthesis 14
Additional Antifungal Compounds 15
Register today for upcoming issues and eBioFiles announcements
at sigma.com/biofiles
New Antibiotics 16
The Antibiotic Web Resource Ready Made Solutions 19
The antibiotic web resource allows you to conveniently browse antibiotic

Antibiotic Selector 21
products by several different categories:
• Alphabetically • Mechanism of Action
• Application • Spectrum of Activity Technical Content:
• Chemical Structure Vicki Caligur, B.Sc. and Chloe McClanahan, B.Sc.
Also get quick access to the full assortment of Ready Made Antibiotic
Solutions and γ–irradiated powders for the most stringent applications.
The antibiotic web resource can be accessed at sigma.com/antibiotics
Antibiotic Selector
The new Antibiotic Selector allows you
to search and browse antibiotics based
on specific applications and activity
spectrum. The online tool provides
detailed usage information about the
chosen antibiotic such as:
• Solubility
• Solution Stability
• Working Concentration
Visit the Antibiotic Selector at sigma.com/antibiotics or see page 21 for

additional information regarding this new online tool.
2
Introduction
Chloe McClanahan
Product Manager, Biochemistry
chloe.mcclanahan@sial.com
This issue of BioFiles provides insight into In addition to our antimicrobial peptides and antifungals, Sigma Life
antibacterial and antifungal resistance. Science is continuously expanding our product offering based on
Antifungal resistance may be just as research interest and customer demand. New antibiotic products
alarming as antibacterial resistance. are described on page 16, while our popular ready made antibiotic
A reported mortality rate for patients solutions are listed on page 19. If you have a new product suggestion
Introduction
with immunity inflicting diseases that for an antibiotic, please visit sigma.com/product_suggestions.
develop resistant fungal infections is 50–90%. Unfortunately,
To help guide researchers
the elevated concern about resistance has not resulted in an
in locating the most
abundance of antibiotics in the pharmaceutical pipeline due to
appropriate antibiotics, we
high developmental costs and commercialization barriers. However,
have created the online
there is currently promising research being done to better
Antibiotic Selector to aid in
understand the mechanisms and interactions of antimicrobial
the selection and usability
peptides and antifungal compounds in order to develop new,
of research antibiotics.
antibiotic drug candidates. Antibiotic Selector
Please see page 21 for an
The article on page 4 provides an informative overview of the Antibiotic Selector tutorial. Additionally, a companion selection
characteristics, mechanisms of action and types of ribosomally poster with application, preparation, usage concentration, solution
synthesized antimicrobial peptides (RAMPs) that either solely stability, and mechanistic information for the most commonly used
provide or contribute to the innate pathogenic defense system for research antibiotics is available. Please visit sigma.com/antibiotics
many species. RAMPs are of growing interest because of continual to use the new Antibiotic Selector.
RAMP discoveries and their lack of resistant isolates. The article
on page 10 provides background information on the structural
components of the fungal cell wall to aid in the understanding of
the damaging functionality of antifungal compounds, along with
a brief synopsis of drug resistance by fungal species. Antimicrobial
peptides and antifungals available from Sigma® Life Science are
found within this issue of BioFiles.
Please visit the BioBlog to see video Special Offer for

on bacterial quorum sensing and
its potential for new antibiotic
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therapeutics. Visit sigmabioblogs.com Register for BioFiles and recieve a
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Metabolic Pathway Chart.
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Our Innovation, Your Research — Shaping the Future of Life Science 3

With bacterial resistance and emerging infectious diseases
becoming potential threats to humans, ribosomally synthesized
antimicrobial peptides have become a promising focus area in
antibiotic research. Antimicrobial peptides are classified as either
non-ribosomally synthesized peptides or ribosomally synthesized
peptides (RAMPs). Non-ribosomally synthesized peptides are found
in bacteria and fungi. These antimicrobial peptides are assembled
by peptide synthetases as opposed to ribosomal-supported
synthesis. Gramicidin, bacitracin, polymyxin B, and vancomycin
are examples of non-ribosomally synthesized antimicrobial

peptides. These antibiotics are proven to be effective research
tools, but compared to RAMPs they are disadvantageous for novel
applications due to emerging bacterial resistance, for example
vancomycin-resistant Staphylococcus aureus and enterococci.
RAMPs are derived from a diverse range of species, from
prokaryotes to humans. Antimicrobial peptides comprise a host’s
natural defense against the daily exposure to millions of potential
pathogens. These peptides may also possess antiviral, antiparasitic,
and antineoplastic activities. Over 500 RAMPs have been described
in the literature. Their unique antibiotic spectrum is determined
by amino acid sequence and structural conformation. RAMPs Figure 1. Antimicrobial peptide perturbation of the bacterial cell wall via the carpet
are gene-encoded peptides consisting of 12-50 amino acids model mode of action.
with very little genetic overlap. A lack of sequence homology RAMPs are ideal candidates for clinical antimicrobial use
between RAMPs is indicative of evolutionary optimization of form because they:
and function in the species environment. RAMPs are typically
1) Are active against antibiotic-resistant isolates
cationic peptides with at least half of the amino acid residues
being hydrophobic and a smaller number of neutral or negatively 2) D
o not select for resistant mutants and have limited
charged residues. Their amphipathic structure with opposing natural bacterial resistance
hydrophobic and lipohphilic faces aids in the perturbation of the 3) A
re synergistic with conventional antibiotics, specifically
bacterial cell wall. against resistant mutants
The mechanism of action of a RAMP involves peptide binding to 4) Are proven to kill bacteria in animal models
the bacterial cell surface, conformational change to the peptide,
aggregation of multiple peptide monomers, and pore formation 5) Kill rapidly
through the bacterial cell wall. RAMPs bind to lipopolysaccharides 6) P rovide benefical, supplementary activities, for example
in the negatively-charged, Gram-negative bacterial outer cell wall sepsis inhibition
or to the acidic polysaccharides of the Gram-positive bacterial
Although RAMPs are ideal clinical candidates, their diverse
outer cell wall. After binding, permeabilization of the bilayer
structural variation makes it difficult to predict RAMP activity
membrane occurs by transient pore creation. Permeabilization
in vivo; therefore, it is challenging to design functional synthetic
leads to a leakage of cell components and cell death. There
mimetics. Small changes in peptide sequence or conformation can
are several models of permeabilization although the precise
lead to major in vivo differences in antimicrobial and cytotoxicity
mechanism is unknown. Three permeabilization models are
levels. An optimal in vitro minimum inhibitory concentration (MIC)
termed barrel-stave, thoroidal, and carpet. Figure 1 depicts
against a range of bacterial organisms is 18 μg/ml. However, it is
bacterial cell wall perturbation by a RAMP.
challenging to predict an ideal in vivo MIC from this in vitro MIC.
In order to obtain MIC, specificity, stability and toxicity information,
novel, synthetic antimicrobial peptides have been designed using
data from RAMP-related, bioinformatic databases (see Table 1).
Production costs, protease susceptibility, and potential resistance
from widespread use are additional concerns in the transition of
RAMP application from a research to clinical setting.
4 sigma.com/lifescience Order: sigma.com/order Technical service: sigma.com/techinfo

Antimicrobial Peptide Databases Information Available Web Site
BAGEL Bacteriocin genome location tool. http://bioinformatics.biol.rug.nl/websoftware/

Molecular Genetics Dept., University of Groningen, The Netherlands bagel/bagel_start.php
PhytAMP Structural information and phylogenetic tree http://phytamp.pfba-lab-tun.org/main.php

ISSBAT Institute, Tunisia and INAF Institute, Laval University, Canada for ~270 natural, plant antimicrobial peptides.
Antimicrobial Peptide Database, Version 2 Structural and functional information for http://aps.unmc.edu/AP/main.html
UNMC Eppley Cancer Center, University of Nebraska Medical Center, USA 1,000+ antibacterial peptides.
SAPD Synthetic antibiotic peptide database. http://oma.terkko.helsinki.fi:8080/~SAPD

Haartman Institute, Helsinki University, Finland
Defensins Knowledgebase Sequence, structural and activity information http://defensins.bii.a-star.edu.sg/

Bioinformatics Institute, Singapore and Singapore Eye Research Institute for ~360 defensins.
Table 1. Antimicrobial Peptide Online Databases
Bacteriocins Insect RAMPs
Bacteriocins are non-pathogenic, antimicrobial peptides or proteins Cecropin is a type of RAMP secreted within insects and active against
secreted by both Gram-positive and Gram-negative bacteria. Gram-negative bacteria. Cecropin A (Cat. No. C6830) is extracted
Bacteriocins prevent the growth of similar bacterial strains but from the hemolymph of the silk moth (Hyalophora cecropia) but has
avoid damaging the host bacteria by selectively killing based also been identified in porcine intestine. Antimicrobial peptides are
on post-transcriptional modification and/or specific immunity often components of insect venoms, for example melittin from bee
mechanisms. Unlike the wide activity spectrum of conventional venom (Cat. No. M2272). It has been proposed that in primitive
antibiotics, bacteriocins have a narrow activity spectrum. insect species RAMPs replace immune system processes, for example
Additionally bacteriocins play a role in the regulation of signaling, cytokine release, that characterize the bactericidal response in higher
virulence, and sporulation. organisms. Drosophila synthesize different antimicrobial peptides
in response to various infecting organisms. Kallio, J. et al. reported
Nisin (Cat. No. N5764) is classified as a Class I, Type A lantibiotic.
that RNAi targeting of several immune response genes in Drosophila
It is produced by Gram-positive, lactic acid fermentation bacteria
caused altered antimicrobial peptide synthesis and identified
and contains several atypical modified amino acids: thioether-
involvement of the JNK signaling pathway in RAMP production.
bridged lanthionine, methyllanthionine, didehydroalanine and
didehydroaminobutyric acid. Class I, Type A lantibiotics are
elongated peptides that exhibit a range of activities including pore
formation in bacterial bilayers while Class I, Type B lantibiotics
are smaller, globular negatively charged or neutral peptides
that inhibit specific enzymes. Class I, Type B lantibiotics include
cinnamycin (Cat. No. C5241) and duramycin (Cat. No. D3168).
An interesting subgroup of the non-lantibiotic bacteriocins is the
Class IIa pediocin-like peptides. Pediocin (Cat. No. P0098) has
been studied for its activity against pathogenic bacteria such as Your gateway to products, services
Listeria monocytogenes. and more life science research
Although the genetic sequences of bacteriocins are not conserved,
bacteriocin genes are often positioned near genes that aid in their
production, for example transporter genes. BAGEL is a bacteriocin
genome location tool developed and maintained by the Molecular
Genetics Department at the University of Groningen, The
Netherlands. This software is available for both academic and
commercial use at http://bioinformatics.biol.rug.nl/websoftware/
bagel/bagel_start.php.
Many of the bacteriocins are being studied for their application
in food preservation. This methodology reduces requirements for
potentially carcinogenic pesticides and heat treatments that reduce
nutritional properties in food.
Bacteriocins may function as alternatives to conventional Read current and previous issues and register to
antibiotics that have been impacted by resistant strains. Millette, receive future BioFiles issues.
M. et al. recently demonstrated that nisin- and pediocin-producing
bacteria reduced intestinal colonization by vancomycin-resistant Visit sigma.com/biofiles
Enterococci in vivo.
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Mammalian RAMPs References:
Pag, U. et al., In vitro activity and mode of action of diastereometric antimicrobial
peptides against bacterial clinical isolates. JAC, 53, 230-239 (2004).
Although bacteriocins, insect, and mammalian RAMPs are similar Papagianni, M., Ribosomally synthesized peptides with antimicrobial properties:
biosynthesis, structure, function, and applications. Biotech. Advances, 21, 465-499 (2003).
in their bactericidal activity, the mammalian RAMPs also function Gunn, J.S., Bacterial modification of LPS and resistance to antimicrobial peptides. J.
Endotoxin Res., 7, 57-62 (2001).
as regulatory molecules in the host species’ immune response. Nicholson, J.K. et al., The challenges of modeling mammalian biocomplexity. Nat.
Biotechnol., 22, 1268-1274 (2004).
Defensins are a group of cationic, mammalian RAMPs that are Palffy, R. et al., On the physiology and pathophysiology of antimicrobial peptides. Mol.
commonly found on the skin, ear, epithelium, tongue, lung, and Med., 15, 51-59 (2009).
Hancock, R. and Chapple, D., Peptide antibiotics. Antimicrob. Agents Chemother., 43,
other surfaces frequently exposed to environmental pathogens. 1317-1323 (1999).
Hancock, R. and Scott, M. The role of antimicrobial peptides in animal defense. PNAS, 97,
Phagocytic and epithelial cells, lymphocytes, and keratinocytes 8856-8861 (2000).
produce defensins. Figure 2 is an immunohistochemical staining Drider, D. et al., The continuing story of class IIa bacteriocins. Microbiol. Mol. Biol. Rev.,
70, 564-582 (2006).
of defensin-5 within respiratory epithelial cells using Prestige
Holtsmark, I. et al., Bacteriocins from plant pathogenic bacteria. FEMS Microbiol. Lett.,
Antibodies® Anti-DEFA5 antibody, produced in rabbit (Cat. No. 280, 1-7 (2007).
Chen, H. and Hoover, D.G. Bacteriocins and their food applications. Comprehensive
HPA015775). Defensins are constitutively expressed and stored Reviews in Food Science and Food Safety, 2, 82-100 (2003).
Galvez, A. et al., Application of bacteriocins in the control of foodborne pathogenic and
in granules without external stimuli. However, increased levels spoilage bacteria. Crit. Rev. Biotechnol., 28, 125-152 (2008).
of expression may be induced by proinflammatory cytokines, Galvez, A. et al., Bacteriocin-based strategies for food biopreservation. Int. J. Food
Microbiol., 120, 51-70 (2007).
exogenous bacterial or LPS treatment. Brumfitt, W. et al., Nisin, alone and combined with peptidoglycan-modulating antibiotics:
activity against methicillin-resistant Staphylococcus aureus and vancomycin-resistant
Like the bacteriocins, defensins consist of variable amino acid enterococci. J. Antimicrob. Chemother., 50, 731-734, (2002).
residue composition. The two classes of defensins are defined Millette, M et al., Capacity of human nisin- and pediocin-producing lactic acid bacteria
to reduce intestinal colonization by vancomycin-resistant enterococci. Appl. Environ.
by structure. The human α-defensins have three intramolecular Microbiol., 74, 1997-2003 (2008).
Montesinos, E., Antimicrobial peptides and plant disease control. FEMS Microbiol. Lett.,
cysteine bonds whereas the larger β-defensins (Cat. Nos. D9565, 270, 1-11 (2007).
β-defensin 1 and D9690, β-defensin 2) consist of three anti- Buckling, A. and Brockhurst, M. Microbiology: RAMP resistance. Nature, 438, 170-171
(2005).
parallel β-sheets and a unique disulfide bridge pattern connecting Kallio, J. et al., Functional analysis of immune response genes in Drosophila identifies JNK
six cysteine residues. In addition to antimicrobial and antiviral pathway as a regulator of antimicrobial peptide gene expression in S2 cells. Microbes and
Infection, 7, 811-819 (2005).
activities, α-defensins inactivate LPS binding, regulate complement Komatsuzawa, H. et al., Innate defences against methicillin-resistant Staphylococcus
aureus (MRSA) infection. J. Pathol., 208, 249-260 (2006).
activation, and function as an adjuvant in mice. β-defensins Meade, K.G. et al., Directed alteration of a novel bovine β-defensin to improve
induce prostaglandin production and play a regulatory role in the antimicrobial efficacy against methicillin-resistant Staphylococcus aureus (MRSA). Int. J.
Antimicrob. Agents, 32, 392-397 (2008).
adaptive immune responses by functioning as chemoattractants Oppenheim, J.J. et al., Roles of antimicrobial peptides such as defensins in innate and
for T lymphocytes as well as for immature dendritic cells via adaptive immunity. Ann. Rheum. Dis., 62, ii17-ii21 (2003).
Yang, D. et al., The role of mammalian antimicrobial peptides and proetins in awakening
signaling through a chemokine receptor. of innate host defenses and adaptive immunity. Cell Mol. Life Sci., 58, 978-989 (2001).
Yang, D. et al., β-Defensins: linking innate and adaptive immunity through dendritic and
T cell CCR6. Science, 286, 525-528 (1999).
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Figure 2. Immunohistochemical staining of human nasopharynx shows cytoplasmic Visit sigma.com/scribd
and membranous positivity in respiratory epithelial cells using Prestige Antibodies®
Anti-DEFA5 (Cat. No. HPA015775).

Bacterial Cell Killing Mechanisms
The diversity of structure within antimicrobial peptides results in an essential, innate defense system for both simple and complex
organisms. Although the antimicrobial peptides have unique structural properties, they can be simply categorized by their killing action.
Antimicrobial peptides typically use one of the following killing mechanisms: cell membrane interference, cell wall synthesis interference,
protein synthesis interference, protein inhibition and nucleic acid inhibition.
Cell Membrane Interference

Name Description Cat. No.
Cecropin A, ≥97% (HPLC), powder Antibacterial peptide originally identified in moths (Hyalophora cecropia) and later in pig intestine. C6830-.1MG
C6830-.5MG
Cecropin B, ≥97% (HPLC), powder Antibacterial peptide originally identified in moths (Hyalophora cecropia) and later in pig intestine. C1796-.1MG
C1796-.5MG
Cecropin P1 Porcine, ≥95% (HPLC), powder Antibacterial peptide originally identified in moths (Hyalophora cecropia) and later in pig intestine. C7927-.1MG
C7927-.5MG
Cinnamycin, >95% (HPLC), solid Cinnamycin (Ro 09-0198) is a tetracylic peptide antibiotic (19 amino acids) that binds specifically to the C5241-1MG
cell surface phosphatidylethanolamine and subsequently induces cytolysis. This is a rare example of a small
peptide binding to a particular lipid (1:1 complex). Cinnamycin belongs to the duramycin-type lantibiotics
and contains the unusual thioether lanthionine amino acids.
Colistin sulfate salt, activity: ≥15,000 units/mg Mode of Action: Binds to lipids on the cell cytoplasmic membrane of Gram-negative bacteria and disrupts C4461-100MG
the cell wall integrity. C4461-1G
Antimicrobial spectrum: Gram-negative bacteria.
Colistin sodium methanesulfonate, Mode of Action: Binds to lipids on the cell cytoplasmic membrane of Gram-negative bacteria and disrupts C1511-10MU
activity: ~11,500 units/mg the cell wall integrity. C1511-100MU
Colistin sodium methanesulfonate, Mode of Action: Binds to lipids on the cell cytoplasmic membrane of Gram-negative bacteria and disrupts 27655-1G
BioChemika, from Bacillus colistinus the cell wall integrity. 27655-5G
Defensin HNP-1 human, ≥80% (HPLC) This is an endogenous antibiotic peptide and monocyte chemotactic peptide produced by human D2043-25UG
neutrophils. Defensins are a family of 3-4 kDa (29-34 amino acids) peptides found in the granules of
mammalian phagocytes. The members of this family are variably arginine-rich and share six conserved
cysteine residues that participate in intramolecular disulfide bonds.
Defensin HNP-2 human, ≥95% (HPLC) This is an endogenous antibiotic peptide and monocyte chemotactic peptide produced by human D6790-25UG
neutrophils. Defensins are a family of 3-4 kDa (29-34 amino acids) peptides found in the granules of
mammalian phagocytes. The members of this famuly are variably arginine-rich and all share 6 conserved
cysteine residues that participate in intramolecular disulfide bonds.
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Cell Membrane Interference, continued
Indolicidin, ≥97% (HPLC) Exhibits potent antimicrobial activity in vitro against bacteria and fungi. I0144-.1MG
Magainin I, ≥97% (HPLC) Antibiotic peptide. Thought to preferentially bind to anionic phospholipids abundant in bacterial M7152-.1MG
membranes with the formation of dynamic peptide-lipid supramolecular pore and cell permeabilization, M7152-.5MG
magainins are positively charged and amphiphatic. Binding to artificial neutral membranes has also been M7152-1MG
demonstrated.
Magainin II, ≥97% (HPLC) Antibiotic peptide. Magainins are positively charged and amphiphatic. Thought to preferentially bind M7402-.1MG
to anionic phospholipids abundant in bacterial membranes with the formation of dynamic peptide-lipid M7402-.5MG
supramolecular pore and cell permeabilization. Binding to artificial neutral membranes has also been M7402-1MG
demonstrated.
Nisin from Lactococcus lactis, 2.5% (balance Antibiotic with bactericidal action on E. coli. Binds to the lipid A portion of bacterial lipopolysaccharides. N5764-1G
sodium chloride and denatured milk solids) Induces pore formation in the membranes of cortex cells from excised sorghum roots. N5764-5G
Mode of Action: Binds to and interferes with the permeability of the cytoplasmic membrane. N5764-25G
Pediocin from Pediococcus acidilactici, Pediocins are class IIa bacteriocins that are produced by Pediococcus sp. They are cationic peptides that P0098-50UG
≥95% (HPLC), buffered aqueous solution 8 show strong activity against pathogenic bacteria such as Listeria monocytogenes, Clostridicum perfringes,
Enterococcus faecalis, and Staphylococcus aureus. This antimicrobial action of pediocins is based on
interaction with the cytoplasmic membrane, resulting in pore formation and cell death.
Polymyxin B solution, BioChemika, - 81271-10ML

1 mg/mL in H2O
Polymyxin B sulfate, Antibiotic with bactericidal action on E. coli. Binds to the lipid A portion of bacterial lipopolysaccharides. P0972-1MU
meets USP testing specifications, powder Induces pore formation in the membranes of cortex cells from excised sorghum roots. P0972-10MU
Mode of Action: Binds to and interferes with the permeability of the cytoplasmic membrane. P0972-50MU
Polymyxin B sulfate salt, Antibiotic with bactericidal action on E. coli. Binds to the lipid A portion of bacterial lipopolysaccharides. P1004-1MU
activity: ≥6,000 USP units/mg Induces pore formation in the membranes of cortex cells from excised sorghum roots. P1004-5MU
Antimicrobial spectrum: Gram-negative bacteria. P1004-25MU
P1004-50MU
Polymyxin B sulfate salt, powder, Antibiotic with bactericidal action on E. coli. Binds to the lipid A portion of bacterial lipopolysaccharides. P4932-1MU
cell culture tested Induces pore formation in the membranes of cortex cells from excised sorghum roots. P4932-5MU
Mode of Action: Binds to and interferes with the permeability of the cytoplasmic membrane.
Polymyxin B sulfate salt, Antibiotic with bactericidal action on E. coli. Binds to the lipid A portion of bacterial lipopolysaccharides. P4119-10MU
Biotechnology Performance Certified Induces pore formation in the membranes of cortex cells from excised sorghum roots. P4119-25MU
Valinomycin, ≥98% (TLC), ≥90% (HPLC), solid K+-selective ionophoric cyclodepsipeptide; potassium ionophore which uncouples oxidative phosphorylation, V0627-10MG
induces apoptosis in murine thymocytes, inhibits NGF-induced neuronal differentiation and antagonizes V0627-25MG
ET-induced vasoconstriction. V0627-100MG
V0627-500MG
Valinomycin, BioChemika, ≥98.0% (TLC) K+-selective ionophoric cyclodepsipeptide; potassium ionophore which uncouples oxidative phosphorylation, 94675-10MG
induces apoptosis in murine thymocytes, inhibits NGF-induced neuronal differentiation and antagonizes 94675-100MG
ET-induced vasoconstriction. 94675-500MG
Valinomycin, Ready Made Solution, K+-selective ionophoric cyclodepsipeptide; potassium ionophore which uncouples oxidative phosphorylation, V3639-5ML
~1 mg/mL in DMSO, 0.2 μm filtered induces apoptosis in murine thymocytes, inhibits NGF-induced neuronal differentiation and antagonizes
ET-induced vasoconstriction.
Cell Wall Synthesis Interference

Bacitracin, from Bacillus licheniformis, Peptide antibiotic. B0125-50KU

activity: ≥50,000 U/g Antimicrobial spectrum: Gram-positive bacteria. B0125-250KU
Mode of Action: Inhibits bacterial cell wall synthesis by inhibiting dephosphorylation of lipid pyrophosphate. B0125-1250KU
Bacitracin, from Bacillus licheniformis, Peptide antibiotic. 11702-5G

BioChemika, activity: ≥60000 U/g (Potency) Antimicrobial spectrum: Gram-positive bacteria. 11702-25G
Mode of Action: Inhibits bacterial cell wall synthesis by inhibiting dephosphorylation of lipid pyrophosphate.
Bacitracin zinc salt, from Bacillus licheniformis, Peptide antibiotic. B5150-250KU

activity: ~70,000 U/g Antimicrobial spectrum: Gram-positive bacteria. B5150-1250KU
Mode of Action: Inhibits bacterial cell wall synthesis by inhibiting dephosphorylation of lipid pyrophosphate.
Vancomycin hydrochloride from Glycopeptide antibiotic V2002-100MG

Streptomyces orientalis, potency: Mode of action: interferes with cell wall synthesis V2002-250MG
≥900 μg per mg (as vancomycin base) Antimicrobial spectrum: Gram-positive bacteria V2002-1G
V2002-5G
Vancomycin hydrochloride from Streptomyces Glycopeptide antibiotic V1764-250MG

orientalis, Biotechnology Performance Certified Mode of action: interferes with cell wall synthesis V1764-1G
Antimicrobial spectrum: Gram-positive bacteria

Protein Synthesis Interference or Inhibition
Actinonin Inhibitor of leucine aminopeptidase. A6671-10MG

A6671-25MG
Amastatin hydrochloride hydrate, ≥97% (HPLC) Amastatin is a slow, tight-binding inhibitor of aminopeptidases. It inhibits cytosolic leucine A1276-250UG
aminopeptidase (EC.3.4.11.1), microsomal aminopeptidase M (EC.3.4.11.2) and bacterial leucine A1276-.5MG
aminopeptidase (EC.3.4.11.10). It is less effective against aminopeptidase A (EC 3.4.11.7), the enzyme A1276-1MG
that converts Angiotensin II to Angiotensin III. Effective concentration: 1-10 μM. A1276-5MG
A1276-10MG
A1276-25MG
Antimycin A from Streptomyces sp. Inhibitor of electron transfer at complex III. Induces apoptosis. A8674-25MG
A8674-50MG
A8674-100MG
Antipain dihydrochloride from microbial source Isolated from a microbial source, antipain hydrochloride is a reversible inhibitor of serine/cysteine A6191-1MG
proteases and some trypsin-like serine proteases. Its action resembles leupeptin; however, its plasmin A6191-5MG
inhibition is less and its cathepsin A inhibition is more than that observed with leupeptin. A6191-25MG
A6191-100MG
Duramycin from Streptoverticillium Polypeptide antibiotic which enhances chloride secretion in airway epithelium; used in studies of D3168-10MG
cinnamoneus, 90-95% cystic fibrosis
Elafin human, >90% (by MS, HPLC and Exhibits co-existant antimicrobial and antiproteolytic activities. E7280-100UG
SDS-PAGE), recombinant, expressed in Antimicrobial spectrum: Gram-positive and Gram-negative bacteria.
Saccharomyces cerevisiae
Gramicidin A from Bacillus brevis, BioChemika, Gramicidin A is a polypeptide antibiotic that forms single ion monovalent cation channels in biological 50845-100MG
≥90% (HPLC) membranes. 50845-500MG
Gramicidin from Bacillus aneurinolyticus (Bacillus Linear polypeptide antibiotic, a mixture of gramicidin A, B, C, and D. Gramicidin D, a channel-forming G5002-100MG
brevis), Linear polypeptide antibiotic complex. ionophore that flip-flops slowly across the membrane is a known Pgp substrate and surprisingly was G5002-500MG
A mixture of gramicidins A, B, C, and D. found to inhibit Pgp ATPase activity. This inhibition was reversed by other Pgp substrates suggesting a G5002-1G
common drug binding site among MDR substrate-type drugs and chemosensitizers. G5002-5G
Gramicidin C from Bacillus brevis, Naturally occuring polypeptide antibiotic with Tyr at position 11; functions as a transmembrane ion channel. 50847-10MG
BioChemika, ~90% (HPLC) 50847-50MG
Thiostrepton from Streptomyces azureus, Peptide antibiotic that prevents the binding of elongation factor G (EF-G) and GTP to the 50S T8902-1G
≥90% (HPLC) ribosomal subunit.
Nucleic Acid Inhibition

Actinomycin D, from Streptomyces sp., An antineoplastic antibiotic that inhibits cell proliferation by forming a stable complex with DNA and A1410-2MG
~98% (HPLC) blocking the movement of RNA polymerase which interferes with DNA-dependent RNA synthesis. Induces A1410-5MG
apoptosis. Potent antitumor agent. For cell culture applications, actinomycin D is used as a selection agent A1410-10MG
and is used in banding techniques to differentiate between different regions of chromosomes. A1410-25MG
A1410-100MG
Actinomycin D, from Streptomyces sp., An antineoplastic antibiotic that inhibits cell proliferation by forming a stable complex with DNA and A4262-2MG
~95% (HPLC) blocking the movement of RNA polymerase which interferes with DNA-dependent RNA synthesis. Induces A4262-5MG
Actinomycin D, ≥95%, from Streptomyces sp., An antineoplastic antibiotic that inhibits cell proliferation by forming a stable complex with DNA and A9415-2MG
cell culture tested blocking the movement of RNA polymerase which interferes with DNA-dependent RNA synthesis. Induces A9415-5MG
Mode of Action: Complexes with DNA and interferes with RNA synthesis.
Actinomycin D–Mannitol, lyophilized powder An antineoplastic antibiotic that inhibits cell proliferation by forming a stable complex with DNA and A5156-1VL
1 mg actinomycin D and 49 mg mannitol per vial blocking the movement of RNA polymerase which interferes with DNA-dependent RNA synthesis. Induces
apoptosis. Potent antitumor agent. For cell culture applications, actinomycin D is used as a selection agent
and is used in banding techniques to differentiate between different regions of chromosomes.

Antifungals
Antifungal compounds have been overshadowed by antibacterials in Antifungal Mechanisms of Action
research interest and application due to the greater impact bacterial
infections have had on health. Resistance to antibacterial drugs Several reviews of antifungal compounds group them into
and the resultant clinical impact is of widespread concern regarding structural classes and have associated certain structures with
public health. However, resistance by pathogenic fungal infections particular modes of actions. Examples of some of the key structures
to drug treatment has become more common in the last 20 years of fungicides are shown in Figure 2. The binding and synthesis of
as well. Some mechanisms of the development of fungal resistance ergosterol, the major cell membrane component, are the targets
have similarities to those of the development of drug resistance in for several antifungal structures. The azoles and triazoles interfere
bacteria, and knowledge of those bacterial mechanisms is being with the ergosterol biosynthesis pathway by inhibiting cytochrome
Antifungals
applied to understanding fungal drug resistance. P450-dependent 14α-demethylase and blocking the oxidative
removal of 14α-methyl from lanosterol. This incomplete processing
Several key antibiotic compounds function by targeting the
of lanosterol results in an increase in ergosterol precursors and
integrity of the cell. Many compounds increase the porosity of the
a decrease in ergosterol, leading to structural changes in the
cell wall or membrane, or interfere with key steps in the synthesis
lipid membrane. Azoles have also been reported to inhibit
of cell walls. While prokaryotic bacteria and eukaryotic fungi do
membrane-surface enzymes and lipid biosynthesis.
not have identical cell wall and membrane components, there
are corresponding lipids and key structural molecules. As a result, Allylamines, of which terbinafine (Cat. No. T8826) is the most
similar to antibacterials, most antifungal compounds work because common example, also block ergosterol biosynthesis, but at an
they directly or indirectly damage the cell wall or cell membrane. earlier step. Terbinatine inhibits the enzyme squalene epoxidase,
which participates in the conversion of squalene to lanosterol. The
The fungal cell wall is composed of multiple layers, with
resulting build-up of squalene is toxic to the fungal cell. A third
mannoproteins being predominantly expressed at the external
structural class, polyenes, increases the permeability of the plasma
surface (see Figure 1). An underlayer of β-glucan creates a
membrane. Amphotericin B (Cat. No. A4888), a polyene with high
supporting matrix for the mannoproteins and provides structural
affinity for sterol binding, is one of the most potent antifungal drugs;
rigidity to the cell wall. The glucan structure is strengthened by
its mechanism produces pores in the membrane surface of the yeast,
frequent β(1→3) and additional β(1→6) linkages and by chitin
resulting in leakage of the cell contents. (Odds, et al., 2003).
interspersed with the β-glucan. Mannoproteins and glucan
make up more than 80% of the cell wall composition, while a. F
chitin represents less than 2%. The plasma membranes of fungi
are primarily composed of ergosterol, analogous to cholesterol
N F N
in animal cells. Since ergosterol and cholesterol have sufficient N
N N
structural differences, the majority of chemicals found to act as N
OH
fungicides target ergosterol biosynthesis or cell membrane porosity
b. CH3 H CH3
and do not cross react with host cells.
N CH3
CH3
Yeast Cell Wall H
Yeast Cell Wall • HCl
Mannoprotein c. OH
OH OH
O
β-Glucan CH3
β-Glucan + Chitin HO O OH OH OH OH O
COOH
CH3 H
Mannoprotein CH2
CH3
O
H3C O OH
Membrane H2N
Nystatin A1
OH
Figure 1. Structure of the yeast cell wall. The wall is primarily composed of d.
mannoproteins and β-glucan that is linked (1→3) and (1→6). Ergosterol is the HO OH
major lipid component of the underlying plasma membrane. HO O H H
H3C
NH
NH CO (CH2)14CH3
N H O
H3C O N CH3
HO H
HO H NH O H OH
O H H N
N
H H OH
HO OH O
H
Figure 2. Examples of antifungal structure classes. a. Fluconazole (triazole)

b. Terbinafine (allylamine) c. Nystatin A1 (polyene) d. Aculeacin A (echinocandin).

In addition to the plasma membrane and its lipid surface, fungicidal Some research reports on antifungals have found greater
compounds may damage the cell wall of yeast. The major cell wall efficacy with combinations of antifungal drugs that use different
component β(1→3) glucan is the target of echinocandins and mechanisms of action. The same process has been applied to other
aculeacins such as aculeacin A (Cat. No. A7603). Echinocandins compounds in looking for ways to overcome fungal resistance. A
are semisynthetic lipopeptides that competitively inhibit β-glucan variety of immunosuppressive compounds, including cyclosporin and
synthetase; the mechanism of action is not well defined but does D-octapeptides (Monk, et al., 2005), have been tested and found
not involve cytochrome P450 inhibition or P-glycoprotein transport to counteract antifungal resistance due to efflux pumps. Cernicka,
(Kauffman and Carver, 2008). et al. screened a synthetic compound library and identified a
Chitin is a trace, critical component of the fungal cell wall, chemical that increased the sensitivity of a drug-resistant strain of
Antifungals
and some inhibitors of chitin synthesis demonstrate antifungal S. cerevisiae to fluconazole (Cernicka, et al., 2007). The compound
activity. Members of this family of antifungals (i.e., polyoxins also increased sensitivity of the pathogenic yeasts Candida albicans
and nikkomycins) have structures analogous to UDP-N-acetyl-D- and Candida glabrata that expressed efflux pumps.
glucosamine (UDP-GlcNAc). This nucleoside phosphate is a glycosyl As drug resistance continues to develop in pathogenic fungi, there
donor substrate for chitin synthesis, and the antifungals act as will be research to find ways to circumvent resistance and identify
competitive substrates to inhibit chitin synthetase (Hector, 1993). next-generation drugs. Understanding the cellular processes
and resistance pathways can be applied to finding alternative
Not all antifungal compounds have known mechanisms of action,
compounds to the well-established azoles that are the prime
and some of them are relatively unique. While there are several
targets of fungal efflux.
antibacterials that function by preventing DNA or RNA replication,
5-fluorocytosine (Cat. No. F7129) is a novel antifungal in that References:
its mechanism of action involves blocking DNA synthesis and Cernicka, J., et al., Chemosensitisation of drug-resistant and drug-sensitive yeast cells
to antifungals. Int. J. Antimicrob. Agents, 29, 170-8 (2007).
inhibiting thymidylate synthetase. Sordarin (Cat. No. S1442) Ghannoum, M.A. and Rice, L.B. Antifungal agents: mode of action, mechanisms of
is one of the few compounds that selectively inhibit fungal resistance, and correlation of these mechanisms with bacterial resistance. Clin. Microbiol.
Rev., 12, 501-17 (1999).
protein synthesis. Other antifungal antibiotics target sphingolipid Gupte, M., et al., Antifungal antibiotics. Appl. Microbiol. Biotechnol., 58, 46-57 (2002).
Hector, R.F. Compounds active against cell walls of medically important fungi. Clin.
biosynthesis and electron transport (Gupte, et al., 2002). The Microbiol. Rev., 6, 1-21 (1993).
mode of action of griseofulvin (Cat. No. G4753) is not completely Kauffman, C.A. and Carver, P.L. Update on echinocandin antifungals. Semin. Respir. Crit.
Care Med., 29, 211-9 (2008).
clear, but it has been speculated that griseofulvin inhibits Katzmann, D.J., et al., Multiple Pdr1p/Pdr3p binding sites are essential for normal
microtubule binding within the mitotic spindle, weakening the cell expression of the ATP binding cassette transporter protein-encoding gene PDR5. J. Biol.
Chem., 271, 23049-54 (1996).
structure (Odds, et al., 2003). Monk, B.C., et al., Surface-active fungicidal D-peptide inhibitors of the plasma membrane
proton pump that block azole resistance. Antimicrob. Agents Chemother., 49, 57-70 (2005).
Monk, B.C. and Goffeau, A. Outwitting multidrug resistance to antifungals. Science, 321,
Drug Resistance by Fungi 367-8 (2008).
Odds, F.C., et al., Antifungal agents: mechanisms of action. Trends Microbiol., 11,
272-9 (2003).
Drug resistance in fungi, especially to azoles, is becoming more Rogers, B., et al., The pleitropic drug ABC transporters from Saccharomyces cerevisiae. J.
Mol. Microbiol. Biotechnol., 3, 207-14 (2001).
prevalent clinically, and the mechanisms of drug resistance are Vanden Bossche, H., et al. Antifungal drug resistance in pathogenic fungi. Med. Mycol.,
36, Supp. 1.,119-28 (1998).
similar to those present in bacteria. Several factors contribute
to multidrug resistance in yeasts, including the mutation of
genes and overexpression of proteins that act as efflux pumps
(Monk and Goffeau, 2008). Fungi contain both ATP-binding
cassette (ABC) transporter and major facilitator superfamily (MFS)
transporter gene families.
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The multidrug resistance process for fungi has been most analyzed
for Saccharomyces cerevisiae, where it is called pleiotropic drug
resistance (PDR) (Rogers, et al., 2001). In S. cerevisiae, point
mutations occur in the genes for the transcription regulatory Scribd Readers!
factors Pdr1p and Pdr3p. These mutations (called “gain-of- Register for BioFiles and recieve a
function” mutations) activated downstream target genes, free Antibiotic Selection poster or
including the ABC transporter genes and MFS transporter genes. IUBMB-Sigma-Nicholson
The products of these genes are efflux pumps that transport Metabolic Pathway Chart.
drug compounds out of the cell, reducing the intracellular
concentration to a sublethal level.

Antifungals that Bind Ergosterol or Inhibit Biosynthesis
Amphotericin B from Streptomyces sp., Polyene antifungal antibiotic from Streptomyces. Affinity for sterols, primarily ergosterols, of fungal cell A4888-100MG
~80% (HPLC), powder membranes. Forms channels in the membranes, causing small molecules to leak out. A4888-250MG
Antimicrobial spectrum: fungi and yeast. A4888-500MG
A4888-1G
A4888-5G
A4888-100G
Amphotericin B from Streptomyces sp., Polyene antifungal antibiotic from Streptomyces. Affinity for sterols, primarily ergosterols, of fungal cell A2411-250MG
~80% (HPLC), cell culture tested membranes. Forms channels in the membranes, causing small molecules to leak out. A2411-1G
Antimicrobial spectrum: fungi and yeast. A2411-5G
Amphotericin B solubilized, powder, Polyene antifungal antibiotic from Streptomyces. Affinity for sterols, primarily ergosterols, of fungal cell A9528-50MG
γ-irradiated, cell culture tested membranes. Forms channels in the membranes, causing small molecules to leak out. A9528-100MG
Antifungals
Antimicrobial spectrum: fungi and yeast. A9528-500MG

Mode of Action: Interferes with fungal membrane permeability by forming channels in the membranes A9528-1G
and causing small molecules to leak out. A9528-5G
Amphotericin B solution, sterile-filtered, Mode of action: Interferes with fungal membrane permeability by forming channels in the membranes A2942-20ML
250 μg/mL in deionized water, and causing small molecules to leak out. A2942-50ML
cell culture tested Antimicrobial spectrum: Yeasts and molds. A2942-100ML
Cerulenin, ~95%, Antibiotic and antifungal. Mode of action: Inhibits fatty acid synthetases, blocking production of fatty C2389-5MG
from Cephalosporium caerulens acids and sterols in both fungi and eukaryotes. C2389-10MG
C2389-50MG
Clotrimazole Specific inhibitor of Ca2+-activated K+ channels. Antifungal azole. Antifungal mode of action: Inhibits C6019-5G
cytochrome P450-dependent 14α-demethylase, which is critical to ergosterol biosynthesis. The C6019-25G
accumulated 14α-methylated sterols change the membrane structure of sensitive fungi, altering cell C6019-100G
membrane permeability.
Dermaseptin from Phyllomedusa sauvagii, Dermaseptin is a cationic, amphipathic antifungal peptide. Mode of action: Lysis of the cell membrane D4671-.1MG
≥97% (HPLC) by interaction with membrane lipids. Highly potent antifungal activity at micromolar concentration. D4671-.5MG
Econazole nitrate salt Econazole is an azole-based antifungal similar to ketoconazole. Its mechanism of action may involve E4632-5G
inhibition of membrane enzymes, including cytochrome P450, and lipid biosynthesis. The bactericidal and E4632-25G
inhibitory effects of several azole antifungal compounds, including econazole, against Mycobacterium E4632-100G
smegmatis has been investigated.
Filipin complex from Streptomyces filipinensis, Filipin is a polyene macrolide antibiotic and antifungal. The antifungal mechanism of action is unclear but F9765-25MG
≥70% (UV) may be due to altering membrane permeability and associated functions via binding to membrane sterols. F9765-50MG
Filipin binds to membrane sterols such as cholesterol, and it both inhibits prion protein (PrP) endocytosis
and causes the release of PrP from the plasma membrane.
Fluconazole, ≥98% (HPLC), solid Fluconazole is an antifungal agent. It is highly selective inhibitor of fungal cytochrome P-450 sterol F8929-100MG
C-14 α-demethyllation. Fluconazole is a potent inhibitor of CYP2C9. Fluconazole interferes with fungal
ergosterol synthesis and downregulates the metallothionein gene.
Itraconazole, ≥98% (TLC) Synthetic broad-spectrum triazole antifungal agent. Mode of action: Inhibits cytochrome P450 dependent I6657-100MG
enzymes including 14α-demethylase. The inhibition results in prevention of the biosynthesis of ergosterol,
a critical fungal cell wall component in fungi.
Ketoconazole, ≥98% (TLC) First generation antifungal azole. Mode of action: Inhibits cytochrome P450-dependent 14α-demethylase, K1003-100MG
which is critical to ergosterol biosynthesis. The accumulated 14α-methylated sterols change the membrane K1003-1G
structure of sensitive fungi, resulting in an altered cell membrane permeability.
(±)-Miconazole nitrate salt Antifungal azole. Mode of action: Inhibits cytochrome P450-dependent 14α-demethylase, which is critical M3512-1G
to ergosterol biosynthesis. The accumulated 14α-methylated sterols change the membrane structure of M3512-5G
sensitive fungi, resulting in an altered cell membrane permeability. Also inhibits peroxidases, which results M3512-25G
in accumulation of peroxide within the cell.
Nystatin preparation, suspension, sterile; Mode of Action: Increases the permeability of the cell membrane of sensitive fungi by binding to sterols. N1638-20ML
aseptically processed, cell culture tested Antimicrobial spectrum: Yeasts and molds. N1638-100ML
Nystatin, activity: ≥4,400 USP units/mg Mode of Action: Increases the permeability of the cell membrane of sensitive fungi by binding to sterols. N3503-5MU
Antimicrobial spectrum: Yeasts and molds. N3503-25MU
Nystatin, powder, cell culture tested Mode of Action: Increases the permeability of the cell membrane of sensitive fungi by binding to sterols. N6261-500KU
Antimicrobial spectrum: Yeasts and molds. N6261-5MU
N6261-25MU
Nystatin, powder, γ-irradiated, Mode of Action: Increases the permeability of the cell membrane of sensitive fungi by binding to sterols. N4014-50MG
cell culture tested Antimicrobial spectrum: Yeasts and molds.
Pimaricin preparation, ~2.5%, An antifungal polyene macrolide that binds specifically to ergosterol and blocks fungal growth. P0440-20ML
aqueous suspension However, unlike nysatin and filipin, pimaricin does not change the permeability of the plasma membrane.
Pimaricin preparation, BioChemika, An antifungal polyene macrolide that binds specifically to ergosterol and blocks fungal growth. 80482-20ML
aqueous suspension 2.5%, sterile, ~90% (N) However, unlike nysatin and filipin, pimaricin does not change the permeability of the plasma membrane.

Pimaricin, from Streptomyces chattanoogensis, An antifungal polyene macrolide that binds specifically to ergosterol and blocks fungal growth. However, P9703-25MG
≥95% (HPLC) unlike nysatin and filipin, pimaricin does not change the permeability of the plasma membrane P9703-50MG
P9703-100MG
Staurosporine from Streptomyces sp., Partially reverses MDR, sensitizing cells with MDR phenotype to cytotoxic agents. Inhibits Pgp S4400-.1MG
≥95% (HPLC), solid phosphorylation. However, functional significance of Pgp phosphorylation is ill defined. Potent inhibitor of S4400-.5MG
phospholipid/calcium-dependent protein kinase. Inhibits the upregulation of VEGF expression in tumor cells. S4400-1MG
Staurosporine from Streptomyces sp., for Partially reverses MDR, sensitizing cells with MDR phenotype to cytotoxic agents. Inhibits Pgp S5921-.1MG
molecular biology, ≥95% (HPLC) phosphorylation. However, functional significance of Pgp phosphorylation is ill defined. Potent inhibitor of S5921-.5MG
phospholipid/calcium-dependent protein kinase. Inhibits the upregulation of VEGF expression in tumor cells. S5921-1MG
Staurosporine solution from Streptomyces sp., Potent inhibitor of phospholipid/calcium-dependent protein kinase. Inhibits the upregulation of VEGF S6942-200UL
Antifungals
Rready Made Solution, 1 mM in DMSO expression in tumor cells.
(100 μg/214 μL), 0.2 μm filtered Potent cell-permeable inhibitor of protein kinase C. Induces apoptosis in Jurkat cells.
Terbinafine hydrochloride, ≥98% 8 Mode of Action: Inhibits squalene epoxidase, preventing biosynthesis of ergosterol. T8826-100MG
Antimicrobial spectrum: Antifungal and antimycotic. Fungicidal against dermatopytes and some yeasts; T8826-250MG
fungistatic against Candida albicans.
Zomepirac sodium salt - Z2625-250MG

Z2625-1G
Z2625-5G
Inhibits β-(1→3)Glucan Synthesis

Aculeacin A, from Aspergillus aculeatus, Aculeacin A, an amphophilic antibiotic, inhibits the biosynthesis of β−glucan by selective blockage of A7603-1MG
≥95% (HPLC) β(1→3) glucan synthase.
Azaserine, ≥98% (TLC) Azaserine is an antibiotic and antifungal; it may also act as a tumor inducer. It is a structural analog of A4142-50MG
glutamine and competes with glutamine in binding to enzymes involved in purine biosynthesis. Azaserine A4142-250MG
inhibits purine biosynthesis by covalently reacting with cysteine residues in the enzyme active sites, such as
in formylglycinamide ribonucleotide amidotransferase and PRPP amidotransferase. Azaserine can induce
DNA damage via the formation of carboxymethylated bases and O6-methylguanine. Secretion of exo-1,3-
β-glucanase and germ-tube formation of Candida albicans were inhibited by azaserine.
Chitin Synthesis Inhibitors

Cycloheximide, BioChemika, ≥93.0% (HPLC) Cycloheximide (CHX) is an antibiotic produced by S. griseus. Its main biological activity is translation 01810-1G
inhibition in eukaryotes resulting in cell growth arrest and cell death. CHX is widely used for selection 01810-5G
of CHX-resistant strains of yeast and fungi, controlled inhibition of protein synthesis for detection of
short-lived proteins and super-induction of protein expression, and apoptosis induction or facilitation of
apoptosis induction by death receptors.
Cycloheximide, from microbial, ≥94% (TLC) Cycloheximide (CHX) is an antibiotic produced by S. griseus. Its main biological activity is translation C7698-1G
inhibition in eukaryotes resulting in cell growth arrest and cell death. CHX is widely used for selection C7698-5G
Cycloheximide, Biotechnology Performance Cycloheximide (CHX) is an antibiotic produced by S. griseus. Its main biological activity is translation C1988-1G
Certified inhibition in eukaryotes resulting in cell growth arrest and cell death. CHX is widely used for selection C1988-5G
Cycloheximide solution, Ready-Made Solution, Cycloheximide (CHX) is an antibiotic produced by S. griseus. Its main biological activity is translation C4859-1ML
microbial, 100 mg/mL in DMSO, 0.2 μm filtered inhibition in eukaryotes resulting in cell growth arrest and cell death. CHX is widely used for selection
Nikkomycin Z from Streptomyces tendae, Nucleoside peptide antibiotic; it inhibits the biosynthesis of chitin in cell walls due to its structural resemblance N8028-5MG
≥90% (HPLC) to UDP-N-acetylglucosamine. Nikkomycin Z has potent antifungal, insecticidal and acaridicial activity.

Interferes with DNA, RNA, or Protein Synthesis
Cordycepin, from Cordyceps militaris Converted to cordycepin 5′-triphosphate. It is incorporated into nucleic acid by poly(A) polymerase, but C3394-10MG
because it lacks a 3′-hydroxyl group, it causes chain termination. It can be used for 3′-end labeling of RNA. C3394-25MG
C3394-100MG
5-Fluorocytosine Nucleoside analog that has antifungal activities. 5-FC is deaminated by cytosine deaminase to product F7129-1G
5-fluorouracil, resulting in RNA miscoding. 5-Fluorocytosine inhibits DNA and RNA synthesis and interferes F7129-5G
with ribosomal protein synthesis.
8-Hydroxyquinoline, crystalline RNA synthesis inhibitor that acts as a fungicide against Trichophyton mentagrophytes, Myrothecium H6878-25G
verrucaria, and Trichoderma viride. The antifungal mechanism of action is not clear but appears to be H6878-100G
structurally related. H6878-500G
Hygromycin B from Streptomyces Mode of Action: Blocks polypeptide synthesis and inhibits elongation. For use in the selection and H3274-50MG
Antifungals
hygroscopicus, powder, cell culture tested, maintenance of prokaryotic and eukaryotic cells. H3274-100MG
insect cell culture tested H3274-5X100MG
H3274-250MG
H3274-1G
Hygromycin B from Streptomyces Mode of Action: Blocks polypeptide synthesis and inhibits elongation. For use in the selection and H7772-50MG
hygroscopicus, lyophilized powder maintenance of prokaryotic and eukaryotic cells. H7772-100MG
H7772-250MG
H7772-1G
Hygromycin B solution from Streptomyces Antibacterial and antifungal. Mode of action: Inhibition of protein synthesis, by inducing the misreading of H0654-250MG
hygroscopicus, ≥60% (HPAE), 45-60 mg/mL the m-RNA template in prokaryotes and eukaryotes. It selectively penetrates cells that have been rendered H0654-500MG
in H2O permeable by virus infection. H0654-1G
Hygromycin B solution from Streptomyces Antibacterial and antifungal. Mode of action: Inhibition of protein synthesis, by inducing the misreading of H5527-250MG
hygroscopicus, ≥60% (HPAE), 45-60 mg/mL the m-RNA template in prokaryotes and eukaryotes. It selectively penetrates cells that have been rendered H5527-500MG
in H2O, γ-irradiated permeable by virus infection. H5527-1G
Kasugamycin hydrochloride from Streptomyces Antifungal aminoglycoside. Mode of action: Inhibits protein synthesis and binding of aminoacyl-SRNA to K4013-10G
kasugaensis, ≥90% (HPLC) the ribosomes in fungi.
Phleomycin from Streptomyces verticillus, Phleomycin is a structurally related form of the antibiotic, bleomycin. Phleomycin blocks S-phase entry in P9564-5MG
powder the cell cycle. While phleomycin can damage DNA, like bleomycin, it is not used as an anticancer agent, but P9564-25MG
rather as a selection agent. The RAD6 DNA repair gene is essential for phleomycin resistance in mutant yeast. P9564-100MG
Sordarin sodium salt, from Sordaria araneosa, Sordarin is an antifungal metabolite possessing a tetracyclic diterpene glycoside structure. It is a highly S1442-5MG
≥98% (HPLC), solid potent inhibitor of eukaryotic protein synthesis with selectivity for the fungal translation machinery. The
elongation factor eEF-2 is the molecular target for sordarin. It blocks ribosomal translocation by stabilizing
the EF2-ribosome complex in a manner similar to that of fusidic acid in the bacterial system. Additional
cellular components (including rpP0, which is an essential protein of the ribosomal large subunit stalk)
are involved in its mechanism of action. Sordarin inhibits in vitro translation in the pathogenic fungi
C. albicans, C. glabrata, and C. neoformans. In addition to its therapeutic potential, sordarin is a useful tool
for the analysis of protein translation events.
Thiolutin, from Streptomyces luteosporeus, Thiolutin is a sulfur-containing antibiotic, which is a potent inhibitor of bacterial and yeast RNA polymerases. T3450-1MG
≥95% (HPLC) It was found to inhibit in vitro RNA synthesis directed by all three yeast RNA polymerases (I, II, and III).
Thiolutin is also an inhibitor of mannan and glucan formation in Saccharomyces cerevisiae and used for
the analysis of mRNA stability. Studies have shown that thiolutin inhibits adhesion of human umbilical vein
endothelial cells (HUVECs) to vitronectin and thus suppresses tumor cell-induced angiogenesis in vivo.
Tubercidin, from Streptomyces tubercidicus, ~95% Toxic adenosine analog with antiviral, antitrypanosomal, and antifungal functions. Mode of action: T0642-10MG
Inhibits multiple metabolic processes, including RNA processing, nucleic acid synthesis, protein synthesis, T0642-50MG
and methylation of tRNA through intracellular incorporation into nucleic acids. Tubercidin acts as a plant T0642-250MG
antifungal, inhibits mammalian SAH hydrolase (SAHH), and blocks purine biosynthesis in Candida famata.
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Additional Antifungal Compounds
Amiodarone hydrochloride, ≥98% Non-selective ion channel blocker with broad fungicidal activity. Amiodarone induces an immediate A8423-1G
influx of Ca2+ in Saccharomyces cerevisiae, followed by mitochondrial fragmentation and cell death. A8423-5G
A8423-10G
Anisomycin from Streptomyces griseolus, Antibiotic isolated from Streptomyces griseolus that inhibits protein synthesis. Acts by inhibiting peptidyl A9789-5MG
~97% (TLC), solid transferase activity in eukaryote ribosomes. Reported to induce apoptosis in a variety of cells including A9789-25MG
promyelocytic leukemia cells, Jurkat cells, ventricular myocytes, and colon adenocarcinoma cells. Initiates A9789-100MG
intracellular signals and immediate early gene induction. Selective signaling agonist. Potent Jun-NH2
terminal kinase (JNK) agonist. Activates mitogen-activated protein (MAP) kinases (JNK/SAPK and p38/RK).
Antiprotozoal agent.
Bafilomycin A1 from Streptomyces griseus, A specific inhibitor of vacuolar type H+-ATPase (V-ATPase) in animal cells, plant cells and microorganisms. B1793-2UG
≥90% (HPLC) B1793-10UG
Antifungals
Cecropin A, ≥97% (HPLC), powder Antibacterial peptide originally identified in moths (Hyalophora cecropia) and later in pig intestine. C6830-.1MG
C6830-.5MG
Griseofulvin, from Penicillium griseofulvum, Antifungal. Mode of action: Disrupts the mitotic spindle structure and inhibits nuclear division. Induces G4753-5G
97.0-102.0% apoptosis in human tumor cell lines. G4753-25G
G4753-50G
Irgasan, BioChemika, ≥97.0% (HPLC) Irgasan is a broad spectrum antimicrobial agent. It is an inhibitor of the enoyl-ACP (acyl-carrier protein) 72779-5G-F
reductase component of type II fatty acid synthase (FAS-II) in bacteria and Plasmodium. It also inhibits 72779-25G-F
mammalian fatty acid synthase (FASN), and may have anticarcinogenic activity.
Iturin A from Bacillus subtilis, ≥90% (HPLC) Iturin A exhibits strong antifungal activity against pathogenic yeast and fungi. It interacts with the I1774-1MG
cytoplasmic membrane of the target cell forming ion conducting pores and its mode of action could I1774-5MG
be attributed to its interaction with sterols and phospholipids. The compound causes the release of
exo-vesicles from human erythrocytes.
Leptomycin B from Streptomyces sp., Leptomycin B is an unsaturated, branched-chain fatty acid, and is an important tool in the study of nuclear L2913-.5UG
5 μg/mL in methanol: water (7:3), ≥95% (HPLC) export. It is a specific inhibitor of proteins containing nuclear export signal. It inhibits nucleo-cytoplasmic L2913-2X.5UG
translocation of molecules such as the HIV-1 Rev protein and Rev-dependent export of mRNA. The addition L2913-5X.5UG
of very small amounts to fibroblasts causes accumulation of MEK in the nucleus. Other proteins that are L2913-10X.5UG
influenced by leptomycin B are actin, c-Abl, cyclin B1, MDM2/p53, IκB, MPF, and PKA. The suggested
inhibition mechanism involves the direct binding of leptomycin B to CRM1, which blocks the binding of
CRM1 to proteins containing the nuclear export signal, via the interaction with cysteine residue in CRM1
control conserved region.
Magnolol, ≥95% (HPLC), from plant 8 Bioactive plant component with antifungal, antibacterial and antioxidant effects. Magnolol also M3445-10MG
demonstrates anti-inflammatory activity by interferring with NF-κB signaling.
Nourseothricin sulfate, BioChemika, ≥85% Antifungal effective against Candida albicans. Candida species transformed with the gene encoding 74667-10MG
(HPLC) nourseothricin acetyltransferase (CaNAT1) were resistant to nourseothricin.
Oligomycin from Streptomyces Macrolide antibiotic; inhibits mitochondrial ATPase and phosphoryl group transfer. O4876-5MG
diastatochromogenes, ~65% oligomycin A O4876-25MG
basis (Composition given on label), ≥90% total O4876-100MG
oligomycins basis (HPLC) O4876-250MG
Rapamycin from Streptomyces hygroscopicus, Rapamycin is a macrocyclic triene antibiotic possessing potent immunosuppressant and anticancer R0395-1MG
≥95% (HPLC), powder activity. It forms a complex with FKBP12 that binds to and inhibits the molecular target of rapamycin
(mTOR). mTOR is a member of the phosphoinositide kinase-related kinase (PIKK) family that enhances
cellular proliferation via the phosphoinositol 3-kinase/Akt signaling pathway. Inhibition of this pathway by
rapamycin blocks downstream elements that result in cell cycle arrest in G1. The effectors of mTOR action
include 4EBP1 and S6K1.
Stigmatellin, BioChemika, ≥95.0% (HPLC) Antibiotic and antifungal from Stigmatella aurantiaca. Inhibits electron transport. Acts at the Qo center of 85865-1MG
the bc1 complex, binds to the heme b1 domain of cytochrome b as well as to the iron-sulfur protein. Used 85865-10MG
in studies on hydroubiquinone-cytochrome c2 oxidoreductase.
Surfactin, from Bacillus subtilis, ≥98% Lipopeptide antibiotic; powerful biosurfactant causes lysis of erythrocytes and bacteria; also a clotting S3523-10MG
inhibitor. S3523-50MG
Tunicamycin from Streptomyces sp. Antibacterial and antifungal. Blocks the formation of protein N-glycosidic linkages by inhibiting the T7765-1MG
transfer of N-acetylglucosamine 1-phosphate to dolichol monophosphate. Inhibits bacterial and eukaryote T7765-5MG
N-acetylglucosamine transferases and prevents formation of N-acetylglucosamine lipid intermediates. T7765-10MG
T7765-50MG

New Antibiotics
Adefovir dipivoxil 8 Cytochalasin B from Drechslera dematioidea 8
9-(2[bis(Pivaloyloxymethoxy)phosphorylmethoxy]ethyl)adenine Phomin CH2

OH
[142340‑99‑6] C20H32N5O8P FW 501.47 [14930‑96‑2] C29H37NO5 FW 479.61 H3C
CH3
H H
Antiviral acyclic nucleoside phosphonate (ANP) analog.
store at: −20°C HN O
OH
A9730-50MG 50 mg O O
A9730-100MG 100 mg
One of a group of fungal metabolites that interfere with a wide variety
of cellular movements. Useful tool for characterizing some of the
Artesunate 8
polymerization properties of actin,† and in studies on cytokinesis.1 Probe for
C19H28O8 FW 384.42 the two hexose-transport systems in rat L6 myoblasts.2
New Antibiotics
Artesunate is a semisynthetic derivative of artemisinin used to treat malaria.1 Lit cited: 1. S. Eperon, J. Protozool. 33, 43 (1986); 2. S.R.Chen, Biochem. J. 251, 3 (1988);
It has also been shown to effective against other parasites such as liver
flukes.2 Artesunate also demonstrates cytotoxic action against cancer cell  Ready Made Solution, 10 mg/mL in DMSO, 0.2 μm filtered
lines of different tumor types.3 Inhibits actin polymerization; inhibits glucose transport.
Lit cited: 1. Prince, R.N., Expert Opin. Investig. Drugs 9, 1815-1827 (2000); 2. Keiser, J., ship: wet ice store at: −20°C
et. al., Antimicrob. Agents Chemother. 57, 1139-1145 (2006); 3. Efferth, T., et. al., Mol. C2743-200UL 200 μL
Pharmacol. 64, 382-394 (2003);
 from Artemisia annua Cytochalasin D 8

store at: Room temp Zygosporin A H2C
A3731-100MG 100 mg [22144‑77‑0] C30H37NO6 FW 507.62 H3C OH
H
H
A3731-500MG 500 mg
CH3
H
HN
Brefeldin A 8 O
O O
γ,4-Dihydroxy-2-(6-hydroxy-1-heptenyl)-4-cyclo O CH3
HO
CH3
H3C O
pentanecrotonic acid λ-lactone; BFA; Cyanein; HO
O
H
Ascotoxin; Decumbin Potent inhibitor of actin polymerization; disrupts actin microfilaments;
[20350‑15‑6] C16H24O4 FW 280.36 H activates the p53-dependent pathways; inhibits smooth muscle contraction;
HO inhibits insulin-stimulated glucose transport.
Disrupts the structure and function of the Golgi apparatus; activator of the R
eady Made Solution, from Zygosporium masonii,
sphingomyelin cycle. 5 mg/mL in DMSO, 0.2 μm filtered
ship: wet ice store at: −20°C
 f rom Penicillium brefeldianum, Ready Made Solution,
10 mg/mL in DMSO, 0.2 μm filtered C2618-200UL 200 μL
ship: wet ice store at: 2-8°C
17-Dimethylaminoethylamino-17-demethoxygel- 8
B5936-200UL 200 μL
danamycin
Cefdinir 8 17-DMAG
[6R-[6α-7beta(Z)]]-7-[[(2-Amino-4-thiazolyl)(hydroxyimino)acetyl]amino]- C32H48N4O8 FW 616.75
3-ethenyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid; 17-DMAG is a more potent water soluble analog of geldanamycin. Inhibits
BMY-28488; FK-482; syn-7-[2-(2-amino-4-thiazolyl)-2-hydroxyimino cancer growth and promotes apoptosis in multiple cell lines. 17-DMAG is a
more potent antitumor agent than 17-AAG.
acetamido]-3-vinyl-3-cephem-4-carboxylic acid
[91832‑40‑5] C14H13N5O5S2 FW 395.41 solubility
An advanced-generation, cephalosporin antibiotic. Used for its excellent DMSO....................................................................................... >25 mg/mL
and well balanced antibacterial activities against gram-positive and ethanol...................................................................................... ~10 mg/mL
gram-negative bacteria. store at: −20°C
solid D5193-1MG 1 mg

solubility
Pediocin from Pediococcus acidilactici 8
dilute HCl..............................................................................slightly soluble
[133108‑87‑9]
mp...................................................................................................... 170 °C
store at: Room temp Pediocins are class IIa bacteriocins that are produced by Pediococcus sp.1
They are cationic peptides that show strong activity against pathogenic
C7118-1G 1 g
bacteria such as Listeria monocytogenes, Clostridicum perfringes,
C7118-5G 5 g Enterococcus faecalis, and Staphylococcus aureus.2 This antimicrobial
action of pediocins is based on interaction with the cytoplasmic membrane,
Clarithromycin 8
resulting in pore formation and cell death.
[81103‑11‑9] C38H69NO13 FW 747.95 Lit cited: 1. Bauer, R. and Dicks, L.M., Mode of action of lipid II-targeting lantibiotics.
Clarithromycin is a macrolide antibiotic. It prevents bacterial growth by Int. J. Food Microbiol. 101, 201-16 (2005); 2. Bhunia, A.K., et al., Purification,
interfering with protein synthesis. Clarithromycin is an acid-stable version of characterization and antimicrobial spectrum of a bacteriocin produced by Pediococcus
acidilactici. J. Appl. Bacteriol. 65, 261-8 (1988);
erythromycin and is particularly effective against gram-negative bacteria.1 It
has a short half-life2, however its metabolite, 14-hydroxy clarithromycin is  ≥95% (HPLC), buffered aqueous solution
nearly twice as active as clarithromycin against certain bacteria.3 concentration............................. 0.1 mg/mL in 0.1 M sodium acetate pH 5.0
Lit cited: 1. Hardy, D.J. et al., Diagn. Microbiol. Infect. Dis. 15, 39-53 (1992); 2. Langtry, ship: dry ice store at: −20°C
H.D., and Brogden, R.N., Drugs 53, 973-1004 (1997); 3. Hardy, D.J, et al., Antimicrob.
Agents Chemother. 32, 1710-1719 (1988); P0098-50UG 50 μg
 ≥95% (HPLC)
C9742-100MG 100 mg
C9742-250MG 250 mg
C9742-1G 1 g

Pefloxacin mesylate dihydrate 8 Rapamycin 8
Pefloxacinium methanesulfonate O O
O
23,27-Epoxy-3H-pyrido[2,1-c][1,4]oxaazacyclohentriacontine solution
dihydrate; Pefloxacine mono F
OH • HO S CH3 C51H79NO13 FW 914.17
methanesulfonate dihydrate; N N
O Rapamycin is a macrocyclic triene antibiotic possessing potent
• 2H2O
3-Quinolinecarboxylic acid, 1-ethyl- N immunosuppressant and anticancer activity. It forms a complex with FKBP12
H3C H3C
6-fluoro-1,4-dihydro-7-(4-methyl-1- that binds to and inhibits the molecular target of rapamycin (mTOR). mTOR
piperazinyl)-4-oxo-, monomethane is a member of the phosphoinositide kinase-related kinase (PIKK) family that
sulfonate, dihydrate enhances cellular proliferation via the phosphoinositol 3-kinase/Akt signaling
C17H20FN3O3 • CH4O3S • 2H2O pathway. Inhibition of this pathway by rapamycin blocks downstream
FW 465.49 elements that result in cell cycle arrest in G1. The effectors of mTOR action
include 4EBP1 and S6K1.
New Antibiotics
Pefloxacin is a synthetic fluoroquinolone that functions an antibacterial
agent. It is an analog of norfloxacin. R
eady Made Solution, 2.5 mg/mL in DMSO (2.74 mM),
Mode of Action: Pefloxacin prevents bacterial DNA replication by inhibiting from Streptomyces hygroscopicus
DNA gyrase. ≥95% (HPLC)
Antimicrobial spectrum: Pefloxacin is highly active against Staphylococcus 0.2 μm filtered
aureus, E. coli, other enterobacteria, and Pseudomonas aeruginosa.1 store at: −20°C
Active against gram-positive bacteria and excellent activity against
R8781-200UL 200 μL
gram-negative bacteria.2
Lit cited: 1. Jones, B.M. et al., Activity of pefloxacin and thirteen other antimicrobial
agents in vitro against isolates from hospital and genitourinary infections J. Antimicrob.
Chemother. 17, 739-746 (1986); 2. Debbia, E. et al., In vitro activity of pefloxacin
against gram-negative and gram-positive bacteria in comparison with other antibiotics.
Chemotherapia 6, 319-326 (1987);
store at: 2-8°C
P0106-10G 10 g
P0106-50G 50 g
Penicillic acid 8 A Perfect Fit!

3-Methoxy-5-methyl-4-oxo-2,5-hexadienoic acid; PA
[90‑65‑3] C8H10O4 FW 170.16
Penicillic acid is a polyketide mycotoxin produced by several species of
Aspergillus and Penicillium species. It induces single and double strand DNA
breaks. Penicillic acid irreversibly inhibits GDP-mannose dehydrogenase
(DMG), an alginate synthesis enzyme. It also inhibits muscle aldose
dehydrogenase, alcohol dehydrogenase, and lactate dehydrogenase.
 ≥98% (HPLC)
solubility
H2O............................................................................................≤10 mg/mL
DMSO....................................................................................... >10 mg/mL
store at: 2-8°C
P0063-10MG 10 mg
P0063-50MG 50 mg
Pirarubicin 8
THP O OH O
[72496‑41‑4] C32H37NO12 FW 627.64 OH
OH
CH3O O OH
O
CH3
O Life Science Innovations and BioFiles
O O offer collaboration and innovation
NH2
from our scientists to you.
Anthracycline antibiotic that is an analog of doxorubicin. Antineoplastic. ■ Life
Science Innovations—new and Download your
Pirarubicin is transported into cells vial a sodium-dependent nucleoside emerging technologies, put forth in a copy of Life Science
transporter.1,2 Innovations at
fresh, unique way, that applies to your
Lit cited: 1. Nagai, K., et al., Pirarubicin is taken up by a uridine-transportable sodium-
area of study sigma.com/innovations
dependent concentrative nucleoside transporter in Ehrlich ascites carcinoma cells. Cancer
Chemother. Pharmacol. 51, 512-8 (2003); 2. Nagai, K., et al., Uptake of the anthracycline
pirarubicin into mouse M5076 ovarian sarcoma cells via a sodium-dependent nucleoside
■ BioFiles—tailored
for the life science Subscribe or download
transport system. Cancer Chemother. Pharmacol. 55, 222-30 (2005); researcher, aligns our vast array of your copy of BioFiles at
products within a relevant research topic sigma.com/biofiles
 ≥95% (HPLC)
ship: wet ice store at: 2-8°C
P8624-10MG 10 mg
sigma-aldrich.com
P8624-25MG 25 mg

Rifaximin 8
Rifacol; 4-Deoxy-4′-methylpyrido[1′,2′-1,2]
Starting a new lab?
OH
imidazo[5,4-c]rifamycin SV O
[80621‑81‑4] C43H51N3O11 FW 785.88 OH OH
OH NH
O
O O N
O N
O O
CH3
Rifaximin is a semisynthetic analog of rifamycin with poor absorptivity.

Mode of action: Inhibition of RNA synthesis.
Antimicrobial spectrum: Aerobic and anaerobic Gram-positive and Gram-
negative bacteria. Active against species of Staphylococcus, Streptococcus
New Antibiotics
and Enterococcus; less active against species of Enterobacteriaceae.1

Lit cited: 1. Gillis, J.C. and Brogden, R.N., Rifaximin. A review of its antibacterial
activity, pharmacokinetic properties and therapeutic potential in conditions mediated by
gastrointestinal bacteria. Drugs 49, 467-84 (1995);
store at: 2-8°C
R9904-1G 1 g
R9904-5G 5 g
Spiramycin adipate 8
Spiramycin hexanedioate
Macrolide antibiotic
Mode of action: Interferes with protein synthesis Let Sigma-Aldrich® help you get it done on time,
Antimicrobial spectrum: mainly Gram-positive bacteria on the spot and on the money.
store at: 2-8°C
S3072-1G 1 g Moving to a new location?
S3072-5G 5 g
Make a good first impression – choose high-quality
Sulfadoxin 8 products at competitive prices from Sigma-Aldrich.
[2447‑57‑6] C12H14N4O4S FW 310.33 O O
HN
S Received your first research grant?
H3CO
N NH2 Focus on your discoveries – not your expenses. Let
H3CO N Sigma-Aldrich help you make the most of your
 ≥95% (TLC) research dollars.
Sulfadoxine is a sulfonamide antibacterial. It inhibits dihydropteroate
synthase (DHPS), an enzyme that transforms 4-aminobenzoic acid (PABA) Easy & Economical Sigma-Aldrich New Lab
in the synthesis of dihydropteroic acid. This enzyme is also a component
of the folate metabolic pathway and is upstream of dihydrofolate Start-Up Program!
reductase (DHFR). Sulfadoxine has been used clinically in combination with
pyrimethamine for malaria treatment.
• Over 100,000 quality biochemical and organic
S7821-10G 10 g
chemical products
S7821-25G 25 g • Savings of up to 70%
• Additional savings as your order value increases
Terbinafine hydrochloride 8
trans-N-(6,6-Dimethyl-2-hepten-4-ylyl)-N- CH3 H CH3

N
Join the Sigma-Aldrich New Lab Start-Up program –
methyl-1-naphthylmethylamine hydrochloride CH3
[78628‑80‑5] C21H25N · HCl FW 327.89 H

CH3 contact your local sales representative for more information.
• HCl
Mode of Action: Inhibits squalene epoxidase, preventing biosynthesis of sigma-aldrich.com

ergosterol.
Antimicrobial spectrum: Antifungal and antimycotic. Fungicidal against
dermatopytes and some yeasts; fungistatic against Candida albicans.
Allylamine derivative.
 ≥98%
T8826-100MG 100 mg
T8826-250MG 250 mg

Ready Made Solutions
Sigma® Life Science Antibiotic Ready Made Solutions arrive at your laboratory as sterile-filtered, ready to use formulations. Ready Made
antibiotic solutions minimize your exposure to potentially harmful powders, reducing your risk as well as saving your time. All Ready
Made Solutions are 0.2 μm filtered for extended shelf life and prevention of bacterial contamination. As with all Sigma Life Science
products, strict quality control measures apply to each Ready Made Solution. For more information on Ready Made Solutions, please visit
sigma.com/readymade
Name Concentration Source Description Cat. No.
Ampicillin 100 mg/mL microbial A β-lactam antibiotic with an amino group side chain attached to the A5354-10ML
penicillin structure. Penicillin derivative that inhibits bacterial cell-wall

synthesis (peptidoglycan cross-linking) by inactivating transpeptidases on
the inner surface of the bacterial cell membrane. Bactericidal only to
growing Escherichia coli. Mode of resistance: Cleavage of β-lactam ring
of ampicillin by β-lactamase. Antimicrobial spectrum: Gram-negative and
Gram-positive bacteria.
Brefeldin A 8 10 mg/mL in DMSO Penicillium Disrupts the structure and function of the Golgi apparatus; activator of the B5936-200UL
brefeldianum sphingomyelin cycle.
Carbenicillin 100 mg/mL in - The antibiotic carbenicillin, an ampicillin analog, is a commonly used C1613-1ML
ethanol/water selection agent that binds and inhibits enzymes involved in the synthesis
of the bacterial cell wall. It is active against most isolates of Pseudomonas
aerogenosa and certain indole-positive Proteus strains that are resistant
to ampicillin. The gene conferring resistance to ampicillin and its analogs,
ampr, codes for the enzyme β-lactamase. Carbenicillin is less sensitive to
β-lactamase than ampicillin. In addition it has a superior stability at low pH.
Experiments have shown that the use of carbenicillin in place of ampicillin
helps prevent overgrowth of satellite colonies. Effective concentration:
50 to 100 μg/ml.
Cycloheximide solution 100 mg/mL in microbial Cycloheximide (CHX) is an antibiotic produced by S. griseus. Its main C4859-1ML
DMSO biological activity is translation inhibition in eukaryotes resulting in
cell growth arrest and cell death. CHX is widely used for selection of
CHX-resistant strains of yeast and fungi, controlled inhibition of protein
synthesis for detection of short-lived proteins and super-induction of protein
expression, and apoptosis induction or facilitation of apoptosis induction by
death receptors.
Cytochalasin B from 10 mg/mL in DMSO Drechslera One of a group of fungal metabolites that interfere with a wide variety C2743-200UL
Drechslera dematioidea 8 dematioidea of cellular movements. Useful tool for characterizing some of the
polymerization properties of actin,† and in studies on cytokinesis. Probe for
the two hexose-transport systems in rat L6 myoblasts.
Inhibits actin polymerization; inhibits glucose transport.
Cytochalasin D 8 5 mg/mL in DMSO Zygosporium Potent inhibitor of actin polymerization; disrupts actin microfilaments; C2618-200UL
masonii activates the p53-dependent pathways; inhibits smooth muscle contraction;
inhibits insulin-stimulated glucose transport.
Ionomycin calcium salt 1 mM in DMSO Streptomyces Ca2+ ionophore that is more effective than A23187 as a mobile ion carrier I3909-1ML
conglobatus for Ca2+.
Puromycin dihydrochloride 10 mg/mL in H2O Streptomyces Puromycin inhibits the growth of a wide range of eukaryotic and prokaryotic P9620-10ML
alboniger cells by interfering with protein synthesis. It allows the selection of cells
expressing the pac gene.

Name Concentration Source Description Cat. No.
Rapamycin 8 2.5 mg/mL in DMSO Streptomyces Rapamycin is a macrocyclic triene antibiotic possessing potent R8781-200UL
(2.74 mM) hygroscopicus immunosuppressant and anticancer activity. It forms a complex with FKBP12
that binds to and inhibits the molecular target of rapamycin (mTOR).
mTOR is a member of the phosphoinositide kinase-related kinase (PIKK)
family that enhances cellular proliferation via the phosphoinositol 3-kinase/
Akt signaling pathway. Inhibition of this pathway by rapamycin blocks
downstream elements that result in cell cycle arrest in G1. The effectors of
mTOR action include 4EBP1 and S6K1.
Spectinomycin 100 mg/mL in Streptomyces sp. Mode of Action: Inhibits protein synthesis (elongation) by interfering with S0692-1ML
DMSO/H2O, 1:1 peptidyl tRNA translocation.
Antimicrobial spectrum: Gram-negative and Gram-positive bacteria
(Gonnococcus only).
Mode of Resistance: Mutation in rpsE (the gene for ribosomal protein S5)
prevents binding of spectinomycin.
Broad spectrum antibiotic produced by the soil bacterium Streptomyces

spectabilis. Spectinomycin inhibits protein synthesis (elongation) by binding
to the bacterial 30S ribosomal subunit and interfering with peptidyl tRNA
translocation. Resistance to spectinomycin is conferred by aminoglycoside-
3′-adenyltransferase gene (aadA).
Spectinomycin is used as a selection marker in plant related transformation
systems. Spectinomycin is also used for amplification of low copy number
plasmid carrying replicons as Col E1, pMB1 (pBR322 and its derivatives), and
p15A/rep (pACYC and its derivatives). The replication of these plasmids relies
on long-lived enzymes supplied by the host. Addition of spectinomycin to the
plasmid containing cells inhibits replication of the host, while the plasmids
continue to replicate for 10-15 hours. The copy number of the plasmid can
increase 100-fold, from 20-30 copies to 3000 copies as in the case of ColE1.
Staurosporine solution from 1 mM in DMSO Streptomyces sp. Potent inhibitor of phospholipid/calcium-dependent protein kinase. Inhibits S6942-200UL
Streptomyces sp. (100 μg/214 μL) the upregulation of VEGF expression in tumor cells.
Potent cell-permeable inhibitor of protein kinase C. Induces apoptosis in
Jurkat cells.
Trichostatin A 8 5 mM in DMSO Streptomyces sp. Trichostatin A is a Streptomyces metabolite, which specifically inhibits T1952-200UL
(0.2 μm-filtered) mammalian histone deacetylase.
Valinomycin ~ 1 mg/mL in DMSO Streptomyces sp. K+-selective ionophore which uncouples oxidative phosphorylation. V3639-5ML
Sigma is Cell Culture
The 3rd edition of the Sigma Cell Culture Manual is a hybrid reference and
product guide designed to be a foundation for your discovery efforts.
■ Extensive cell culture technical information and formulas

■ Our most popular cell culture products and equipment
■ Invaluable tool to help advance your research goals
Order your copy of the 2008–2009 Cell Culture Manual by visiting sigma.com/ccmanual
sigma-aldrich.com

Antibiotic Selector
The Antibiotic Selector enables researchers to spend ■ uickly find the best antibiotic for your research.
Q
more time on their research discoveries and less time
■ etailed application and usage information.
D
seeking established antibiotic information. Link to nearly
200 antibiotics for contamination prevention, genetic marker ■ Link to easy online ordering.
selection and cell biology studies. Access application, activity
spectrum, and usage data derived from a combination of For more information, visit sigma.com/antibiotics
hands on experience, peer-reviewed literature, and Sigma
quality control analysis.
The following tutorial provides instructions on how to:

■S
earch, browse and filter for an antibiotic that meets your
research requirements
■A
ccess solvent, solution storage and working concentration
recommendations for each antibiotic
■ Link to current pricing, availability and easy, online ordering
Search- Search by
antibiotic name
If you already know your antibiotic of interest, search the Application and
name then select it from the results to access the detailed usage information
usage and application information.

Close the window to return to the main antibiotic selector
window. Start a new search by clicking the red “New
Search” button.
Browse-
To browse antibiotics by application, select one of the
following from the Application menu: cell culture, plant
cell culture, selection agent, antineoplastic agent.
To browse antibiotics by activity spectrum, select one of the
following from the Activity Spectrum menu: Gram +, Gram -,
Mycobacteria, Yeast, Molds, Mycoplasmas and Viruses.
You can further refine your results by first browsing the
antibiotics by application and then filtering the results by
a specific activity spectrum or first browsing by activity
Browse by Browse by
spectrum and then filtering the results by application. application activity spectrum
Click on your antibiotic of interest from the list to access
the detailed usage information.
Once you have completed a search, be sure to start a
new search by clicking the red “New Search” button
before starting a new search or browsing by application
or activity spectrum.
Price and
availability
Online Ordering-
The Antibiotic Selector links to an online ordering page for
each antibiotic product. The online ordering page displays
current pricing and availability information.
We expect the Antibiotic Selector to be a beneficial tool for you and your colleagues. To access the Antibiotic Selector,
please visit sigma.com/antibiotics
The Bioactive Nutrient Explorer
Your connection to plant defense compounds
Designed to help you locate the chemicals and kits needed to support your antimicrobial-
related phytochemical research, the Bioactive Nutrient Explorer is an Internet-based tool n L ink Antibacterial,
that identifies the compounds found in a specific plant and arranges them by chemical Antifungal, and
Antiviral Actions to
family and class. You can also search for compounds having a similar chemical structure or Specific Plants
for plants containing a specific compound. When you’ve found the product you need, a n eview Antimicrobial-
R
simple mouse click links you to our easy online ordering system. Related Chemical
Families: Tannins,
Terpenoids, Phenols,
Flavones, and Alkaloids.
Bioactive Nutrient Explorer n L ocate Defense

Phytochemicals Found
Helping Scientists Connect Bioactives to Botanicals in Specific Plants
Visit sigma-aldrich.com/nutrition
sigma-aldrich.com
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Life Science

See page 3 for

Peptides perturbing bacterial cell wall and

Your gateway to Biochemicals and Reagents

✓ future issues Inhibits β-(1→3)Glucan Synthesis 13

✓ eBioFiles email notifications Chitin Synthesis Inhibitors 13

The Antibiotic Web Resource Ready Made Solutions 19

The antibiotic web resource allows you to conveniently browse antibiotic

The antibiotic web resource can be accessed at sigma.com/antibiotics

Visit the Antibiotic Selector at sigma.com/antibiotics or see page 21 for

Please visit the BioBlog to see video Special Offer for

Our Innovation, Your Research — Shaping the Future of Life Science 3

are examples of non-ribosomally synthesized antimicrobial

4 sigma.com/lifescience Order: sigma.com/order Technical service: sigma.com/techinfo

BAGEL Bacteriocin genome location tool. http://bioinformatics.biol.rug.nl/websoftware/

PhytAMP Structural information and phylogenetic tree http://phytamp.pfba-lab-tun.org/main.php

SAPD Synthetic antibiotic peptide database. http://oma.terkko.helsinki.fi:8080/~SAPD

Defensins Knowledgebase Sequence, structural and activity information http://defensins.bii.a-star.edu.sg/

Table 1. Antimicrobial Peptide Online Databases

Our Innovation, Your Research — Shaping the Future of Life Science 5

Special Offer for

6 sigma.com/lifescience Order: sigma.com/order Technical service: sigma.com/techinfo

Cell Membrane Interference

New Antibodies Catalog

Our Antibody Collection is Expanding—

 Validation using a variety of applications—WB, IHC, IF, ELISA

Request your free copy at sigma.com/09abcat

Our Innovation, Your Research — Shaping the Future of Life Science

Our Innovation, Your Research — Shaping the Future of Life Science 7

Polymyxin B solution, BioChemika, - 81271-10ML

Cell Wall Synthesis Interference

Bacitracin, from Bacillus licheniformis, Peptide antibiotic. B0125-50KU

Bacitracin, from Bacillus licheniformis, Peptide antibiotic. 11702-5G

Bacitracin zinc salt, from Bacillus licheniformis, Peptide antibiotic. B5150-250KU

Vancomycin hydrochloride from Glycopeptide antibiotic V2002-100MG

Vancomycin hydrochloride from Streptomyces Glycopeptide antibiotic V1764-250MG

8 sigma.com/lifescience Order: sigma.com/order Technical service: sigma.com/techinfo

Actinonin Inhibitor of leucine aminopeptidase. A6671-10MG

Nucleic Acid Inhibition

Our Innovation, Your Research — Shaping the Future of Life Science 9

Figure 2. Examples of antifungal structure classes. a. Fluconazole (triazole)

10 sigma.com/lifescience Order: sigma.com/order Technical service: sigma.com/techinfo

Special Offer for

Our Innovation, Your Research — Shaping the Future of Life Science 11

Antimicrobial spectrum: fungi and yeast. A9528-500MG

12 sigma.com/lifescience Order: sigma.com/order Technical service: sigma.com/techinfo

Zomepirac sodium salt - Z2625-250MG

Inhibits β-(1→3)Glucan Synthesis

Chitin Synthesis Inhibitors

Our Innovation, Your Research — Shaping the Future of Life Science 13

Special Offer for

14 sigma.com/lifescience Order: sigma.com/order Technical service: sigma.com/techinfo

Our Innovation, Your Research — Shaping the Future of Life Science 15

9-(2[bis(Pival­oyl­oxy­methoxy)phos­phor­yl­methoxy]ethyl)adenine Phomin CH2

 from Artemisia annua Cyto­chalasin D 8

solid D5193-1MG 1 mg

16 sigma.com/lifescience Order: sigma.com/order Technical service: sigma.com/techinfo

Peni­cil­lic acid 8 A Perfect Fit!

Our Innovation, Your Research — Shaping the Future of Life Science 17

Rifaximin is a semisynthetic analog of rifamycin with poor absorptivity.

and Enterococcus; less active against species of Enterobacteriaceae.1

trans-N-(6,6-Dimethyl-2-hepten-4-ylyl)-N- CH3 H CH3

[78628‑80‑5] C21H25N · HCl FW 327.89 H

Validation using a variety of applications—WB, IHC, IF, ELISA

9-(2[bis(Pivaloyloxymethoxy)phosphorylmethoxy]ethyl)adenine Phomin CH2

 from Artemisia annua Cytochalasin D 8

Penicillic acid 8 A Perfect Fit!

Bioactive Nutrient Explorer n L ocate Defense