Antimicrobial peptides: premises and promises - PubMed (original) (raw)
Review
Antimicrobial peptides: premises and promises
K V R Reddy et al. Int J Antimicrob Agents. 2004 Dec.
Abstract
Antimicrobial peptides (AMPs) are an important component of the natural defences of most living organisms against invading pathogens. These are relatively small (< 10kDa), cationic and amphipathic peptides of variable length, sequence and structure. During the past two decades several AMPs have been isolated from a wide variety of animals, both vertebrates and invertebrates, and plants as well as from bacteria and fungi. Most of these peptides are obtained from different sources like macrophages, neutrophils, epithelial cells, haemocytes, fat body, reproductive tract, etc. These peptides exhibit broad-spectrum activity against a wide range of microorganisms including Gram-positive and Gram-negative bacteria, protozoa, yeast, fungi and viruses. A few peptides have also been found to be cytotoxic to sperm and tumour cells. AMPs are classified based on the three dimensional structural studies carried out with the help of NMR. The peptides are broadly classified into five major groups namely (a) peptides that form alpha-helical structures, (b) peptides rich in cysteine residues, (c) peptides that form beta-sheet, (d) peptides rich in regular amino acids namely histatin, arginine and proline and (e) peptides composed of rare and modified amino acids. Most of these peptides are believed to act by disrupting the plasma membrane leading to the lysis of the cell. AMPs have been found to be excellent candidates for developing novel antimicrobial agents and a few of these peptides show antimicrobial activity against pathogens causing sexually transmitted infection (STI), including HIV/HSV. Peptides, namely magainin and nisin have been shown to demonstrate contraceptive properties in vitro and in vivo. A few peptides have already entered clinical trials for the treatment of impetigo, diabetic foot ulcers and gastric helicobacter infections. In this review, we discuss the source, structures and mode of action with special reference to therapeutic considerations of various AMPs.
Comment in
- Clinical development of antimicrobial peptides.
Andrès E, Dimarcq JL. Andrès E, et al. Int J Antimicrob Agents. 2005 May;25(5):448-9. doi: 10.1016/j.ijantimicag.2005.02.003. Int J Antimicrob Agents. 2005. PMID: 15848303 No abstract available.
Similar articles
- Antimicrobial peptides: new candidates in the fight against bacterial infections.
Toke O. Toke O. Biopolymers. 2005;80(6):717-35. doi: 10.1002/bip.20286. Biopolymers. 2005. PMID: 15880793 Review. - Antimicrobial peptides as microbicidal contraceptives: prophecies for prophylactics--a mini review.
Yedery RD, Reddy KV. Yedery RD, et al. Eur J Contracept Reprod Health Care. 2005 Mar;10(1):32-42. doi: 10.1080/13625180500035124. Eur J Contracept Reprod Health Care. 2005. PMID: 16036297 Review. - Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp.
Chou HT, Kuo TY, Chiang JC, Pei MJ, Yang WT, Yu HC, Lin SB, Chen WJ. Chou HT, et al. Int J Antimicrob Agents. 2008 Aug;32(2):130-8. doi: 10.1016/j.ijantimicag.2008.04.003. Epub 2008 Jun 30. Int J Antimicrob Agents. 2008. PMID: 18586467 - Structure-activity relationships of de novo designed cyclic antimicrobial peptides based on gramicidin S.
Lee DL, Hodges RS. Lee DL, et al. Biopolymers. 2003;71(1):28-48. doi: 10.1002/bip.10374. Biopolymers. 2003. PMID: 12712499 - Resistance to antimicrobial peptides in Gram-negative bacteria.
Gruenheid S, Le Moual H. Gruenheid S, et al. FEMS Microbiol Lett. 2012 May;330(2):81-9. doi: 10.1111/j.1574-6968.2012.02528.x. Epub 2012 Mar 12. FEMS Microbiol Lett. 2012. PMID: 22339775 Review.
Cited by
- AMPGAN v2: Machine Learning-Guided Design of Antimicrobial Peptides.
Van Oort CM, Ferrell JB, Remington JM, Wshah S, Li J. Van Oort CM, et al. J Chem Inf Model. 2021 May 24;61(5):2198-2207. doi: 10.1021/acs.jcim.0c01441. Epub 2021 Mar 31. J Chem Inf Model. 2021. PMID: 33787250 Free PMC article. - Molecular Characterization and Phylogenetic Analysis of a Histone-Derived Antimicrobial Peptide Teleostin from the Marine Teleost Fishes, Tachysurus jella and Cynoglossus semifasciatus.
Chaithanya ER, Philip R, Sathyan N, Anil Kumar PR. Chaithanya ER, et al. ISRN Mol Biol. 2013 Mar 3;2013:185807. doi: 10.1155/2013/185807. eCollection 2013. ISRN Mol Biol. 2013. PMID: 27335674 Free PMC article. - The application of antimicrobial peptides as growth and health promoters for swine.
Xiao H, Shao F, Wu M, Ren W, Xiong X, Tan B, Yin Y. Xiao H, et al. J Anim Sci Biotechnol. 2015 May 7;6(1):19. doi: 10.1186/s40104-015-0018-z. eCollection 2015. J Anim Sci Biotechnol. 2015. PMID: 26019864 Free PMC article. - Oviduct-specific expression of human neutrophil defensin 4 in lentivirally generated transgenic chickens.
Liu T, Wu H, Cao D, Li Q, Zhang Y, Li N, Hu X. Liu T, et al. PLoS One. 2015 May 28;10(5):e0127922. doi: 10.1371/journal.pone.0127922. eCollection 2015. PLoS One. 2015. PMID: 26020529 Free PMC article. - Gas Chromatography-Mass Spectrometry Profiling of Volatile Metabolites Produced by Some Bacillus spp. and Evaluation of Their Antibacterial and Antibiotic Activities.
Koilybayeva M, Shynykul Z, Ustenova G, Waleron K, Jońca J, Mustafina K, Amirkhanova A, Koloskova Y, Bayaliyeva R, Akhayeva T, Alimzhanova M, Turgumbayeva A, Kurmangaliyeva G, Kantureyeva A, Batyrbayeva D, Alibayeva Z. Koilybayeva M, et al. Molecules. 2023 Nov 12;28(22):7556. doi: 10.3390/molecules28227556. Molecules. 2023. PMID: 38005278 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Medical
Miscellaneous