Antimicrobial peptides

From Wikipedia, the free encyclopedia

Various structures of antimicrobial peptides

Antimicrobial peptides (AMPs), also called host defense peptides (HDPs) are part of the innate
immune response found among all classes of life. Fundamental differences exist between
prokaryotic and eukaryotic cells that may represent targets for antimicrobial peptides. These
peptides are potent, broad spectrum antibiotics which demonstrate potential as novel therapeutic
agents. Antimicrobial peptides have been demonstrated to kill Gram negative and Gram
positive bacteria, enveloped viruses, fungi and even transformed or cancerous cells.[1] Unlike the
majority of conventional antibiotics it appears as though antimicrobial peptides may also have the
ability to enhance immunity by functioning as immunomodulators.
Marine fish sources have high levels of antimicrobial compounds with in vivo testing confirming the
efficacy of fish peptides used in food/feed ingredients.[2]

Contents
[hide]

1Structure
2Activities
3Immunomodulation
4Mode of action
5Therapeutic potential
o 5.1Anticancer
6Selectivity
o 6.1Factors
o 6.2Mechanism
o 6.3Control
7Bacterial resistance
8Examples
9Bioinformatics
10See also
 11Footnotes
12References
13External links

Structure[edit]
Antimicrobial peptides are a unique and diverse group of molecules, which are divided into
subgroups on the basis of their amino acid composition and structure.[3]Antimicrobial peptides are
generally between 12 and 50 amino acids. These peptides include two or more positively charged
residues provided by arginine, lysine or, in acidic environments, histidine, and a large proportion
(generally >50%) of hydrophobic residues.[4][5][6] The secondary structures of these molecules follow 4
themes, including i) -helical, ii) -stranded due to the presence of 2 or more disulfide bonds, iii) -
hairpin or loop due to the presence of a single disulfide bond and/or cyclization of the peptide chain,
and iv) extended.[7] Many of these peptides are unstructured in free solution, and fold into their final
configuration upon partitioning into biological membranes. It contains hydrophilic amino acid
residues aligned along one side and hydrophobic amino acid residues aligned along the opposite
side of a helical molecule.[3] This amphipathicity of the antimicrobial peptides allows them to partition
into the membrane lipid bilayer. The ability to associate with membranes is a definitive feature of
antimicrobial peptides[8][9] although membrane permeabilization is not necessary. These peptides
have a variety of antimicrobial activities ranging from membrane permeabilization to action on a
range of cytoplasmic targets.

Type characteristic AMPs

rich in glutamic and

Anionic peptides Maximin H5 from amphibians, Dermcidin from humans
aspartic acids

Cecropins, andropin, moricin, ceratotoxin and melittin from

Linear cationic - insects, Magainin, dermaseptin, bombinin, brevinin-1,
lack in cysteine
helical peptides esculentins and buforin II from amphibians, CAP18 from
rabbits, LL37from humans

rich in proline,
Cationic peptide
arginine, abaecin, apidaecins from honeybees, prophenin from
enriched for specific
phenylalanine, pigs, indolicidin from cattle.
amino acid
glycine, tryptophan

Anionic and cationic 1 bond:brevinins, 2 bonds:protegrin from

peptides that contain contain 1~3 disulfide pig, tachyplesins from horseshoe crabs, 3
cysteine and form bond bonds:defensins from humans, more than 3:drosomycin in
disulfide bonds fruit flies

Activities[edit]
The modes of action by Antimicrobial peptides

The modes of action by which antimicrobial peptides kill microbes are varied,[10] and may differ for
different bacterial species.[11] Some antimicrobial peptides kill both bacteria and fungi, e.g., psoriasin
kills E. coli and several filamentous fungi.[12] The cytoplasmic membrane is a frequent target, but
peptides may also interfere with DNA and protein synthesis, protein folding, and cell wall
synthesis.[10]The initial contact between the peptide and the target organism is electrostatic, as most
bacterial surfaces are anionic, or hydrophobic, such as in the antimicrobial peptide Piscidin. Their
amino acid composition, amphipathicity, cationic charge and size allow them to attach to and insert
into membrane bilayers to form pores by barrel-stave, carpet or toroidal-pore mechanisms.
Alternately, they may penetrate into the cell to bind intracellular molecules which are crucial to cell
living.[13] Intracellular binding models includes inhibition of cell wall synthesis, alteration of the
cytoplasmic membrane, activation of autolysin, inhibition of DNA, RNA, and protein synthesis, and
inhibition of certain enzymes. However, in many cases, the exact mechanism of killing is not known.
One emerging technique for the study of such mechanisms is dual polarisation interferometry.[14][15] In
contrast to many conventional antibiotics these peptides appear to be bactericidal[1] instead
of bacteriostatic. In general the antimicrobial activity of these peptides is determined by measuring
the minimal inhibitory concentration (MIC), which is the lowest concentration of drug that inhibits
bacterial growth.[16]

Immunomodulation[edit]
In addition to killing bacteria directly they have been demonstrated to have a number
of immunomodulatory functions that may be involved in the clearance of infection, including the
ability to alter host gene expression, act as chemokines and/or induce chemokine production,
inhibiting lipopolysaccharide induced pro-inflammatory cytokine production, promoting wound
healing, and modulating the responses of dendritic cells and cells of the adaptive immune response.
Animal models indicate that host defence peptides are crucial for both prevention and clearance of
infection. It appears as though many peptides initially isolated as and termed "antimicrobial peptides"
have been shown to have more significant alternative functions in vivo (e.g. hepcidin[17]).

Mode of action[edit]
Several methods have been used to determine the mechanisms of antimicrobial peptide
activity.[11][13] In particular, solid-state NMR studies have provided an atomic-level resolution
explanation of membrane disruption by antimicrobial peptides.[18][19]

Methods Applications

Microscopy to visualize the effects of antimicrobial peptides on microbial cells

to detect loss of intracellular potassium (an indication that bacterial

Atomic emission spectroscopy
membrane integrity has been compromised)

to measure ability of antimicrobial peptides to permeabilize membrane

Fluorescent dyes
vesicles

Ion channel formation to assess the formation and stability of an antimicrobial-peptide-induced pore

Circular dichroism and to measure the orientation and secondary structure of an antimicrobial
orientated circular dichroism peptide bound to a lipid bilayer

Dual Polarization
to measure the different mechanisms of antimicrobial peptides
Interferometry

to measure the secondary structure, orientation and penetration of

Solid-state NMR spectroscopy antimicrobial peptides into lipid bilayers in the biologically relevant liquid-
crystalline state

to measure the diffraction patterns of peptide-induced pores within

Neutron and X-ray diffraction
membranes in oriented multilayers or liquids

Therapeutic potential[edit]
These peptides are excellent candidates for development as novel therapeutic agents and
complements to conventional antibiotic therapy because they generally have a broad range of
activity, are bactericidal[1] as opposed to bacteriostatic and require a short contact time to induce
killing. A number of naturally occurring peptides and their derivatives have been developed as novel
anti-infective therapies for conditions as diverse as oral mucositis, lung infections associated
with cystic fibrosis (CF), cancer,[20] and skin and wound infections.[11] Pexiganan has been shown to
be useful to treat infection related diabetic foot ulcer.
A major limitation to the therapeutic potential is the possibility of bacteria developing resistance to
the peptides, and particularly if that produces a resistance to the body's own immune system use of
those peptides. That is, providing a lot of the peptides as a therapeutic agent makes it easier for
resistance to evolve; unlike antibiotic resistance, however, resistance to antimicrobial peptides
mimicking those produced by humans can make the bacteria more resistant to the body's own
immune system rather than just the antibiotic.[21]
Antimicrobial peptides have been successively incorporated into topical therapeutics.[citation needed] A
major challenge associated with systemic delivery of an antimicrobial peptides is their susceptibility
to proteolytic degradation. That is, the peptides are quickly broken down when introduced in the
bloodstream.[citation needed]
Anticancer[edit]
Some of the cecropins (e.g. cecropin A, and cecropin B) have anticancer properties and are called
anticancer peptides (ACPs).[22]:3 Hybrid ACPs based on Cecropin A have been studied for anticancer
properties.[22]:7.1

Selectivity[edit]
In the competition of bacterial cells and host cells with the antimicrobial peptides, antimicrobial
peptides will preferentially interact with the bacterial cell to the mammalian cells, which enables them
to kill microorganisms without being significantly toxic to mammalian cells.[23] Selectivity is a very
important feature of the antimicrobial peptides and it can guarantee their function as antibiotics in
host defense systems.
Factors[edit]
There are some factors that are closely related to the selectivity property of antimicrobial peptides,
among which the cationic property contributes most. Since the surface of the bacterial membranes is
more negatively charged than mammalian cells, antimicrobial peptides will show different affinities
towards the bacterial membranes and mammalian cell membranes.[24]
In addition, there are also other factors that will affect the selectivity. Its well known
that cholesterol is normally widely distributed in the mammalian cell membranes as a membrane
stabilizing agents but absent in bacterial cell membranes; and the presence of these cholesterols will
also generally reduce the activities of the antimicrobial peptides, due either to stabilization of the lipid
bilayer or to interactions between cholesterol and the peptide. So the cholesterol in mammalian cells
will protect the cells from attack by the antimicrobial peptides.[25]
Besides, the transmembrane potential is well-known to affect peptide-lipid interactions.[26] There's an
inside-negative transmembrane potential existing from the outer leaflet to the inner leaflet of the cell
membranes and this inside-negative transmembrane potential will facilitate membrane
permeabilization probably by facilitating the insertion of positively charged peptides into membranes.
By comparison, the transmembrane potential of bacterial cells is more negative than that of normal
mammalian cells, so bacterial membrane will be prone to be attacked by the positively charged
antimicrobial peptides.
Similarly, it is also believed that increasing ionic strength,[25] which in general reduces the activity of
most antimicrobial peptides, contributes partially to the selectivity of the antimicrobial peptides by
weakening the electrostatic interactions required for the initial interaction.
Molecular Basis of Cell Selectivity of Antimicrobial Peptides

Mechanism[edit]
The cell membranes of bacteria are rich in acidic phospholipids, such
as phosphatidylglyceroland cardiolipin.[23][27] These phospholipid headgroups are heavily negatively
charged. Therefore, the outmost leaflets of the bilayer which is exposed to the outside of the
bacterial membranes are more attractive to the attack of the positively charged antimicrobial
peptides. So the interaction between the positive charges of antimicrobial peptides and the
negatively charged bacterial membranes is mainly the electrostatic interactions, which is the major
driving force for cellular association. In addition, since antimicrobial peptides form structures with a
positively charged face as well as a hydrophobic face, there are also some hydrophobic interactions
between the hydrophobic regions of the antimicrobial peptides and the zwitterionicphospholipids
(electrically neutral) surface of the bacterial membranes, which act only as a minor effect in this
case.
In contrast, the outer part of the membranes of plants and mammals is mainly composed of lipids
without any net charges since most of the lipids with negatively charged headgroups are principally
sequestered into the inner leaflet of the plasma membranes.[24] Thus in the case of mammalian cells,
the outer surfaces of the membranes are usually made of
zwitterionic phosphatidylcholine and sphingomyelin, even though a small portion of the membrane's
outer surfaces contain some negatively charged gangliosides. Therefore, the hydrophobic interaction
between the hydrophobic face of amphipathic antimicrobial peptides and the zwitterionic
phospholipids on the cell surface of mammalian cell membranes plays a major role in the formation
of peptide-cell binding.[28] However, the hydrophobic interaction is relatively weak when compared to
the electrostatic interaction, thus, the antimicrobial peptides will preferentially interact with bacterial
membranes.[citation needed]
Dual polarisation interferometry has been used in vitro to study and quantify the association to
headgroup, insertion into the bilayer, pore formation and eventual disruption of the membrane.[29][30]
Control[edit]
A lot of effort has been put into controlling cell selectivity. For example, attempts have been made to
modify and optimize the physicochemical parameters of the peptides to control the selectivities,
including net charge, helicity, hydrophobicity per residue (H), hydrophobic moment () and the angle
subtended by the positively charged polar helix face ().[26] Other mechanisms like the introduction of
D-amino acids and fluorinated amino acids in the hydrophobic phase are believed to break the
secondary structure and thus reduce hydrophobic interaction with mammalian cells. It has also been
found that ProNlys substitution in Pro-containing -turn antimicrobial peptides was a promising
strategy for the design of new small bacterial cell-selective antimicrobial peptides with intracellular
mechanisms of action.[31] It has been suggested that direct attachment of magainin to the substrate
surface decreased nonspecific cell binding and led to improved detection limit for bacterial cells such
as Salmonella and E. coli.[32]

Bacterial resistance[edit]
Bacteria use various resistance strategies to avoid antimicrobial peptide killing.[13] Some
microorganisms alter net surface charges. Staphylococcus aureustransports D-alanine from the
cytoplasm to the surface teichoic acid which reduces the net negative charge by introducing basic
amino groups.[33] S. aureus also modifies its anionic membranes via MprF with L-lysine, increasing
the positive net charge.[33] The interaction of antimicrobial peptides with membrane targets can be
limited by capsule polysaccharide of Klebsiella pneumoniae.[34] Alterations occur in Lipid
A. Salmonella species reduce the fluidity of their outer membrane by increasing hydrophobic
interactions between an increased number of Lipid A acyl tails by adding myristate to Lipid A with 2-
hydroxymyristate and forming hepta-acylated Lipid A by adding palmitate. The increased
hydrophobic moment is thought to retard or abolish antimicrobial peptide insertion and pore
formation. The residues undergo alteration in membrane proteins. In some Gram-negative bacteria,
alteration in the production of outer membrane proteins correlates with resistance to killing by
antimicrobial peptides.[35] Nontypeable Hemophilus influenzae transports AMPs into the interior of the
cell, where they are degraded. And H. influenzae remodels its membranes to make it appear as if
the bacterium has already been successfully attacked by AMPs, protecting it from being attacked by
more AMPs.[36] ATP-binding cassette transporters import antimicrobial peptides and the resistance-
nodulation cell-division efflux pump exports antimicrobial peptides.[37]Both transporters have been
associated with antimicrobial peptide resistance. Bacteria produce proteolytic enzymes, which may
degrade antimicrobial peptides leading to their resistance.[38] Outer membrane vesicles produced by
Gram-negative bacteria bind the antimicrobial peptides and sequester them away from the cells,
thereby protecting the cells.[39] The outer membrane vesicles are also known to contain various
proteases, peptidases and other lytic enzymes, which may have a role in degrading the extracellular
peptide and nucleic acid molecules, which if allowed to reach to the bacterial cells may be
dangerous for the cells. Cyclic-di-GMP signaling had also been involved in the regulation
of antimicrobial peptide resistance in Pseudomonas aeruginosa[40]
While these examples show that resistance can evolve naturally, there is increasing concern that
using pharmaceutical copies of antimicrobial peptides can make resistance happen more often and
faster. In some cases, resistance to these peptides used as a pharmaceutical to treat medical
problems can lead to resistance, not only to the medical application of the peptides, but to the
physiological function of those peptides.[21] Further research is needed to determine if this will lead to
greater harm than benefit from the use of certain antimicrobial peptides.[citation needed]

Examples[edit]
Antimicrobal peptides are produced by all known species, including peptides from bacteria, from
fungi, from hydra, insects (mastoparan, poneratoxin, cecropin,moricin, melittin and others),[41] frogs
(magainin, dermaseptin and others),[42] and mammals (for
example, cathelicidins, defensins and protegrins). Research has increased in recent years to
develop artificially-engineered mimics of antimicrobial peptides such as SNAPPs, in part due to the
prohibitive cost of producing naturally-derived AMPs.[43]

Bioinformatics[edit]
Several bioinformatic databases exist to catalogue antimicrobial peptides such as CAMP, CAMP
release 2 (Collection of sequences and structures of antimicrobial peptides) [44] the Antimicrobial
Peptide Database (http://aps.unmc.edu/AP/main.php), LAMP, BioPD (see external links) and ADAM
(A Database of Anti-Microbial peptides) [45] (http://bioinformatics.cs.ntou.edu.tw/adam/). The
Antimicrobial peptide databases may be divided into two categories on the basis of the source of
peptides it contains, as specific databases and general databases. These databases have various
tools for antimicrobial peptides analysis and prediction. For example, CAMP contains AMP
prediction, feature calculator, BLAST search, clustalW, VAST, PRATT, Helical wheel etc. In addition,
ADAM allows users to search or browse through AMP sequence-structure relationships. Both
PeptideRanker [46] and PeptideLocator [47] allow for the prediction of antimicrobial peptides (see
external links).

See also[edit]
Cathelicidin
Aurein
Copsin
Peripheral membrane proteins
Virtual colony count

Footnotes[edit]
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Iwama; R. E. W. Hancock (May 2000). "Antimicrobial Peptides Protect
Coho Salmon from Vibrio anguillarum Infections".Applied and
Environmental Microbiology. 66 (5): 19281932. PMC 101435
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3. ^ Jump up to:a b Yeaman & Yount 2003
4. Jump up^ Papagianni 2003
5. Jump up^ Sitaram & Nagaraj 2002
6. Jump up^ Drr, Sudheendra & Ramamoorthy 2006
7. Jump up^ Dhople, Krukemeyer & Ramamoorthy 2006
8. Jump up^ Hancock & Rozek 2002
9. Jump up^ Varkey J, Singh S, Nagaraj R (2006)."Antibacterial activity
of linear peptides spanning the carboxy-terminal -sheet domain of
arthropod defensins". Peptides. 27 (11): 2614
2623.PMID 16914230.doi:10.1016/j.peptides.2006.06.010.
10. ^ Jump up to:a b Nguyen LT, Haney EF, Vogel HJ (2011). "The
expanding scope of antimicrobial peptide structures and their modes
of action". Trends in Biotechnology. 29 (9): 464
472. PMID 21680034.doi:10.1016/j.tibtech.2011.05.001.
11. ^ Jump up to:a b c O'Driscoll NH, Labovitiadi O, Cushnie TP, Matthews
KH, Mercer DK, Lamb AJ (2013). "Production and evaluation of an
antimicrobial peptide-containing wafer formulation for topical
application". Current Microbiology. 66 (3): 271
278.PMID 23183933. doi:10.1007/s00284-012-0268-3.
12. Jump up^ Hein, Kyaw Zaw; Takahashi, Hitoshi; Tsumori, Toshiko;
Yasui, Yukihiko; Nanjoh, Yasuko; Toga, Tetsuo; Wu, Zhihong;
Grtzinger, Joachim; Jung, Sascha (2015-10-20). "Disulphide-reduced
 psoriasin is a human apoptosis-inducing broad-spectrum
fungicide". Proceedings of the National Academy of Sciences of the
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Sharon, Park Yoonkyung, Hahm Kyung-Soo, Isabel Aguilar Marie.
"The effect of acyl chain structure and bilayer phase state on the
binding and insertion of HPA3 onto a supported lipid
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Gehman John D., Separovic Frances, Aguilar Marie-Isabel (2010).
"Real time quantitative analysis of lipid disordering by aurein 1.2
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30. Jump up^ Tzong-Hsien Lee, Kristopher Hall, Adam Mechler, Lisandra
Martin, Jonathan Popplewell, Gerry Ronan, Marie-Isabel Aguilar
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External links[edit]
ADAM (A Database of Anti-Microbial peptides) at ntou.edu.tw
CAMP:Collection of Anti-Microbial Peptides at National Institute for
Research in Reproductive Health (NIRRH)
CAMP 2 at NIRRH
LAMP at NCBI
BioPD at bjmu.edu
Antimicrobial Peptide Database at unmc.edu
UMich Orientation of Proteins in Membranes classes/type-3 -
Calculated spatial positions of peptides in the lipid bilayer
Antimicrobial Cationic Peptides at the US National Library of
Medicine Medical Subject Headings (MeSH)
PeptideLocator Prediction of functional peptides, including
antimicrobial peptides, in a protein sequence
PeptideRanker Bioactive peptide, including antimicrobial peptide,
prediction

[show]

Antimicrobial peptides: Granulocyte granule contents

[show]

Pore-forming toxins (TC 1C)

Categories:
Antimicrobial peptides
Immunology
Immune system
 Peripheral membrane proteins
Insect immunity
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