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      Antimicrobial Peptides for Therapeutic Applications: A Review

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          Abstract

          Antimicrobial peptides (AMPs) have been considered as potential therapeutic sources of future antibiotics because of their broad-spectrum activities and different mechanisms of action compared to conventional antibiotics. Although AMPs possess considerable benefits as new generation antibiotics, their clinical and commercial development still have some limitations, such as potential toxicity, susceptibility to proteases, and high cost of peptide production. In order to overcome those obstacles, extensive efforts have been carried out. For instance, unusual amino acids or peptido-mimetics are introduced to avoid the proteolytic degradation and the design of short peptides retaining antimicrobial activities is proposed as a solution for the cost issue. In this review, we focus on small peptides, especially those with less than twelve amino acids, and provide an overview of the relationships between their three-dimensional structures and antimicrobial activities. The efforts to develop highly active AMPs with shorter sequences are also described.

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          Most cited references 58

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          The expanding scope of antimicrobial peptide structures and their modes of action.

          Antimicrobial peptides (AMPs) are an integral part of the innate immune system that protect a host from invading pathogenic bacteria. To help overcome the problem of antimicrobial resistance, cationic AMPs are currently being considered as potential alternatives for antibiotics. Although extremely variable in length, amino acid composition and secondary structure, all peptides can adopt a distinct membrane-bound amphipathic conformation. Recent studies demonstrate that they achieve their antimicrobial activity by disrupting various key cellular processes. Some peptides can even use multiple mechanisms. Moreover, several intact proteins or protein fragments are now being shown to have inherent antimicrobial activity. A better understanding of the structure-activity relationships of AMPs is required to facilitate the rational design of novel antimicrobial agents. Copyright © 2011 Elsevier Ltd. All rights reserved.
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            Peptide antibiotics.

             R. Hancock (1997)
            The era of the "classical antibiotic" may be over. The emergence of resistance has seen to that. Yet no truly novel class of antibacterial agent has come on the market in the past 30 years. Currently there is great interest in peptide antibiotics, especially the cationic peptides. Thousands of such molecules have been synthesised and just a few are entering clinical trials. Because they kill bacteria quickly by the physical disruption of cell membranes, peptide antibiotics may not face the rapid emergence of resistance.
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              A review of antimicrobial peptides and their therapeutic potential as anti-infective drugs.

              Antimicrobial peptides (AMPs) are an essential part of innate immunity that evolved in most living organisms over 2.6 billion years to combat microbial challenge. These small cationic peptides are multifunctional as effectors of innate immunity on skin and mucosal surfaces and have demonstrated direct antimicrobial activity against various bacteria, viruses, fungi, and parasites. This review summarizes their progress to date as commercial antimicrobial drugs for topical and systemic indications. Literature review. Despite numerous clinical trials, no modified AMP has obtained Food & Drug Administration approval yet for any topical or systemic medical indications. While AMPs are recognized as essential components of natural host innate immunity against microbial challenge, their usefulness as a new class of antimicrobial drugs still remains to be proven.
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                Author and article information

                Journal
                Molecules
                Molecules
                molecules
                Molecules
                MDPI
                1420-3049
                18 October 2012
                October 2012
                : 17
                : 10
                : 12276-12286
                Affiliations
                [1 ]College of Pharmacy, Ajou University, Suwon 443-749, Korea
                [2 ]Department of Biotechnology, College of Biomedical and Health Science, Konkuk University, Chungju, Chungbuk 380-701, Korea
                [3 ]Center for Structural Biology and Departments of Biochemistry and Pharmacology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA
                [4 ]Faculty of Biology, National University of Mongolia, Ulaanbaatar Box 377, Mongolia
                [5 ]Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 151-742, Korea
                Author notes
                [* ] Author to whom correspondence should be addressed; Email: lbj@ 123456nmr.snu.ac.kr ; Tel.: +82-2-880-7869; Fax: +82-2-872-3632.
                Article
                molecules-17-12276
                10.3390/molecules171012276
                6268056
                23079498
                721f55e4-cabc-453e-a0f5-d0cfaf015e57
                © 2012 by the authors; licensee MDPI, Basel, Switzerland.

                This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

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