Elsevier

Peptides

Volume 37, Issue 2, October 2012, Pages 207-215
Peptides

Review
Overview on the recent study of antimicrobial peptides: Origins, functions, relative mechanisms and application

https://doi.org/10.1016/j.peptides.2012.07.001Get rights and content

Abstract

Antimicrobial peptides (AMPs), which are produced by several species including insects, other animals, micro-organisms and synthesis, are a critical component of the natural defense system. With the growing problem of pathogenic organisms resistant to conventional antibiotics, especially with the emergence of NDM-1, there is increased interest in the pharmacological application of AMPs. They can protect against a broad array of infectious agents, such as bacteria, fungi, parasite, virus and cancer cells. AMPs have a very good future in the application in pharmaceuticals industry and food additive. This review focuses on the AMPs from different origins in these recent years, and discusses their various functions and relative mechanisms of action. It will provide some detailed files for clinical research of pharmaceuticals industry and food additive in application.

Highlights

Antimicrobial peptides (AMPs) produced by several species including insects, other animals, micro organisms and synthesis, are a critical component of the natural defense system. ► With the growing problem of pathogenic organisms resistant to conventional antibiotics, especially with the emergence of NDM-1, there is increased interest in the pharmacological application of AMPs. ► They can protect against a broad array of infectious agents, such as bacteria, fungi, parasite, virus and cancer cells. ► AMPs have a good future in the application in pharmaceuticals industry and food additive.

Introduction

Antimicrobial peptides (AMPs) are gene-encoded, ribosomally synthesized polypeptides. They usually have the common characteristics: small peptide (30–60 aa), strong cationic (pI 8.9–10.7), heat-stable (100 °C, 15 min), no drug fastness and no effect on eukaryotic cell. The natural AMPs have been isolated and characterized from practically all-living organisms, ranging from prokaryotes to humans. The AMPs produced by bacteria are also termed ‘bacteriocins’ [5], [6]. AMPs usually work against bacteria that are closely related to the producer strains in prokaryotes, while they play a key role in innate immunity in eukaryotes. These peptides are produced by several species including bacteria, insects, plants, vertebrates and they have been recognized as ancient evolutionary molecules that have been effectively preserved in mammals [1], [50].

In 2008, a Swedish patient of Indian origin traveled to New Delhi (India) and acquired a urinary tract infection caused by a carbapenem-resistant Klebsiella pneumoniae strain that typed to the sequence type 14 complex. The isolate, K. pneumoniae 05–506, was shown to possess a metallo-β-lactamase (MBL) but was negative for previously known MBL genes [103]. This enzyme hydrolysing all β-lactams except aztreonam is commonly identified in multidrug-resistant isolates and we name this kind of organisms as NDM-1 (It stands for New Delhi metallo-beta-lactamase 1). It is coded by blaNDM-1 or NDM-1 gene which encodes, 269 amino acids containing protein, with molecular mass of approx 27.5 kDa [15]. The spread of these organisms has prompted widespread concern because some of them are resistant to the vast majority of antimicrobial agents [51], [77]. Since antibiotic resistance to conventional antibiotics is occurring, there is increased interest in the pharmacological application of AMPs. An updated database of AMPs is available on line at: http://aps.unmc.edu/AP/main.php [95].

The significant advantage of AMPs resides in the global mechanism of their action, which is remarkably different from that of conventional antibiotics. Usage of AMPs will gain widespread increase since more and more bacteria may develop the ability to resist conventional antibiotics due to the abuse of these drugs worldwide. This article will summarize the recent AMPs and their relative mechanisms from various origins.

Section snippets

Origins of AMPs

AMPs can be commonly classified into four groups according to their origins. They are from insects, other animals, synthesis and genetically engineered microorganism. To date more than 1500 AMPs of different origins have been reported [34].

Different functions of AMPs

AMPs display multifunctional properties with implications as potential therapeutic agents. They exhibit rapid killing, often within minutes in vitro, and a broad spectrum of activity against Gram-positive and Gram-negative bacteria, fungi, parasites, enveloped viruses and tumor cells. In these several years, they have been termed “natural antibiotics”, because they are active against a large spectrum of microorganisms including bacteria, filamentous fungi, protozoan and metazoan parasites. It

Conclusions

Drug resistance is a major problem in antibacterial chemotherapy, and AMPs may solve this problem in the future. AMPs are currently in the spotlight as potential candidates to overcome bacterial resistance to conventional antibiotics. Many AMPs have multi-functions such as antibacterial, antifungal and anti-cancer activities. Because they are able to rapidly kill broad range of infectious agents and modulate both innate and adaptive immunity, considerable efforts have been made to exploit their

Acknowledgment

This work is supported by major project of Guangdong Province Department of Education (cgzhzd0710).

References (113)

  • Y.S. Choi et al.

    Cloning and expression profiling of four antibacterial peptide genes from the bumblebee Bombus ignites

    Comp Biochem Physiol B Biochem Mol Biol

    (2008)
  • B. Charroux et al.

    Bacterial detection by Drosophila peptidoglycan recognition proteins

    Microbes Infect

    (2009)
  • J.M. Cerón et al.

    The antimicrobial peptide cecropin A induces caspase-independent cell death in human promyelocytic leukemia cells

    Peptides

    (2010)
  • Y.Q. Chen et al.

    Expression of a cytotoxic cationic antibacterial peptide in Escherichia coli using two fusion partners

    Protein Expr Purif

    (2008)
  • Y.Q. Chen et al.

    A cationic amphiphilic peptide ABP-CM4 exhibits selective cytotoxicity against leukemia cells

    Peptides

    (2010)
  • M. Cassone et al.

    Scope and limitations of the designer proline-rich antibacterial peptide dimer, A3-APO, alone or in synergy with conventional antibiotics

    Peptides

    (2008)
  • L. Cohen et al.

    Drosomycin, an innate immunity peptide of Drosophila melanogaster, interacts with the fly voltage-gated sodium channel

    J Biol Chem

    (2009)
  • A.D. Cirac et al.

    The molecular basis for antimicrobial activity of pore-forming cyclic peptides

    Biophys J

    (2011)
  • B. Duvic et al.

    Cecropins as a marker of Spodoptera frugiperda immunosuppression during entomopathogenic bacterial challenge

    J Insect Physiol

    (2012)
  • P. Díaz et al.

    Antibacterial activity of six novel peptides from Tityus discrepans scorpion venom. A fluorescent probe study of microbial membrane Na+ permeability changes

    Toxicon

    (2009)
  • R.E. Dean et al.

    A carpet-based mechanism for direct antimicrobial peptide activity against vaccinia virus membranes

    Peptides

    (2010)
  • E. Guaní-Guerra et al.

    Antimicrobial peptides: general overview and clinical implications in human health and disease

    Clin immunol

    (2010)
  • C. Graham et al.

    Histamine-releasing and antimicrobial peptides from the skin secretions of the dusky gopher frog, Rana sevosa

    Peptides

    (2006)
  • V.M. Gomes et al.

    Purification and characterization of a novel peptide with antifungal activity from Bothrops jararaca venom

    Toxicon

    (2005)
  • C.I. Guerreiro et al.

    Escherichia coli expression and purification of four antimicrobial peptides fused to a family 3 carbohydrate-binding module (CBM) from Clostridium thermocellum

    Protein Expr Purif

    (2008)
  • B. Gao et al.

    Characterization of two linear cationic antimalarial peptides in the scorpion Mesobuthus eupeus

    Biochimie

    (2010)
  • J. Herbinière et al.

    Armadillidin: a novel glycine-rich antibacterial peptide directed against Gram-positive bacteria in the woodlouse Armadillidium vulgare (Terrestrial Isopod, Crustacean)

    Dev Comp Immunol

    (2005)
  • L.X. Hou et al.

    Inhibition of foodborne pathogens by Hf-1, a novel antibacterial peptide from the larvae of the house Xy (Musca domestica) in medium and orange juice

    Food Control

    (2007)
  • Y. Hu et al.

    An antimicrobial peptide with trypanocidal activity characterized from Glossina morsitans morsitans

    Insect Biochem Mol Biol

    (2005)
  • M. Imamura et al.

    Multipeptide precursor structure of acaloleptin A isoforms, antibacterial peptides from the Udo longicorn beetle, Acalolepta luxuriosa

    Dev Comp Immunol

    (2009)
  • P. Jiravanichpaisal et al.

    Antibacterial peptides in hemocytes and hematopoietic tissue from freshwater crayfish Pacifastacus leniusculus: characterization and expression pattern

    Dev Comp Immunol

    (2007)
  • F. Jin et al.

    Expression of recombinant hybrid peptide cecropin A(1–8)-magainin 2(1–12) in Pichia pastoris: purification and characterization

    Protein Expr Purif

    (2006)
  • F. Jean-Francois et al.

    Pore formation induced by an antimicrobial peptide: electrostatic effects

    Biophys J

    (2008)
  • K. Konno et al.

    Decoralin, a novel linear cationic alpha-helical peptide from the venom of the solitary eumenine wasp Oreumenes decoratus

    Peptides

    (2007)
  • C. Kim et al.

    Evidence of pores and thinned lipid bilayers induced in oriented lipid membranes interacting with the antimicrobial peptides, magainin-2 and aurein-3.3

    Biochim Biophys Acta

    (2009)
  • S. Liu et al.

    Crystal structure of mastoparan from Polistes jadwagae at 1.2 A resolution

    J Struct Biol

    (2007)
  • J. Lu et al.

    Isolation characterization and anti-cancer activity of SK84, a novel glycine-rich antimicrobial peptide from Drosophila virilis

    Peptides

    (2010)
  • J.R. Leite et al.

    Phylloseptins: a novel class of anti-bacterial and anti-protozoan peptides from the Phyllomedusa genus

    Peptides

    (2005)
  • F.T. Lundy et al.

    Antimicrobial activity of truncated alpha-defensin (human neutrophil peptide (HNP)-1) analogues without disulphide bridges

    Mol Immunol

    (2008)
  • M.D. Lavine et al.

    Immune challenge differentially affects transcript abundance of three antimicrobial peptides in hemocytes from the moth Pseudoplusia includens

    Insect Biochem Mol Biol

    (2005)
  • J.L. Lopes et al.

    Disruption of Saccharomyces cerevisiae by Plantaricin 149 and investigation of its mechanism of action with biomembrane model systems

    Biochim Biophys Acta

    (2009)
  • Y. Lan et al.

    Structural contributions to the intracellular targeting strategies of antimicrobial peptides

    Biochim Biophys Acta

    (2010)
  • M. Minaba et al.

    Evolution of ASABF (Ascaris suum antibacterial factor)-type antimicrobial peptides in nematodes: putative rearrangement of disulfide bonding patterns

    Dev Comp Immunol

    (2009)
  • P. Mak et al.

    A different repertoire of Galleria mellonella antimicrobial peptides in larvae challenged with bacteria and fungi

    Dev Comp Immunol

    (2010)
  • I. Mulero et al.

    The antimicrobial peptides piscidins are stored in the granules of professional phagocytic granulocytes of fish and are delivered to the bacteria-containing phagosome upon phagocytosis

    Dev Comp Immunol

    (2008)
  • G. Maróti et al.

    Natural roles of antimicrobial peptides in microbes, plants and animals

    Res Microbiol

    (2011)
  • M. Mihajlovic et al.

    Antimicrobial peptides bind more strongly to membrane pores

    Biochim Biophys Acta

    (2010)
  • I.K. Maurya et al.

    Antifungal activity of novel synthetic peptides by accumulation of reactive oxygen species (ROS) and disruption of cell wall against Candida albicans

    Peptides

    (2011)
  • P. Méndez-Samperio

    The human cathelicidin hCAP18/LL-37: a multifunctional peptide involved in mycobacterial infections

    Peptides

    (2010)
  • M. Niu et al.

    The molecular design of a recombinant antimicrobial peptide CP and its in vitro activity

    Protein Expr Purif

    (2008)
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