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      Short Cationic Peptidomimetic Antimicrobials

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          Abstract

          The rapid growth of antimicrobial resistance against several frontline antibiotics has encouraged scientists worldwide to develop new alternatives with unique mechanisms of action. Antimicrobial peptides (AMPs) have attracted considerable interest due to their rapid killing and broad-spectrum activity. Peptidomimetics overcome some of the obstacles of AMPs such as high cost of synthesis, short half-life in vivo due to their susceptibility to proteolytic degradation, and issues with toxicity. This review will examine the development of short cationic peptidomimetics as antimicrobials.

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          Mode of action of membrane active antimicrobial peptides.

          Yechiel Shai (2002)
          Water-membrane soluble protein and peptide toxins are used in the defense and offense systems of all organisms, including plants and humans. A major group includes antimicrobial peptides, which serve as a nonspecific defense system that complements the highly specific cell-mediated immune response. The increasing resistance of bacteria to conventional antibiotics stimulated the isolation and characterization of many antimicrobial peptides for potential use as new target antibiotics. The finding of thousands of antimicrobial peptides with variable lengths and sequences, all of which are active at similar concentrations, suggests a general mechanism for killing bacteria rather than a specific mechanism that requires preferred active structures. Such a mechanism is in agreement with the "carpet model" that does not require any specific structure or sequence. It seems that when there is an appropriate balance between hydrophobicity and a net positive charge the peptides are active on bacteria. However, selective activity depends also on other parameters, such as the volume of the molecule, its structure, and its oligomeric state in solution and membranes. Further, although many studies support that bacterial membrane damage is a lethal event for bacteria, other studies point to a multihit mechanism in which the peptide binds to several targets in the cytoplasmic region of the bacteria.
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            Acquired Antibiotic Resistance Genes: An Overview

            Angela H A M van Hoek, Dik Mevius, Beatriz Guerra … (2011)
            In this review an overview is given on antibiotic resistance (AR) mechanisms with special attentions to the AR genes described so far preceded by a short introduction on the discovery and mode of action of the different classes of antibiotics. As this review is only dealing with acquired resistance, attention is also paid to mobile genetic elements such as plasmids, transposons, and integrons, which are associated with AR genes, and involved in the dispersal of antimicrobial determinants between different bacteria.
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              Multifunctional cationic host defence peptides and their clinical applications.

              Amy Yeung, Shaan Gellatly, Robert E. W. Hancock (2011)
              With the rapid rise in the emergence of bacterial strains resistant to multiple classes of antimicrobial agents, there is an urgent need to develop novel antimicrobial therapies to combat these pathogens. Cationic host defence peptides (HDPs) and synthetic derivatives termed innate defence regulators (IDRs) represent a promising alternative approach in the treatment of microbial-related diseases. Cationic HDPs (also termed antimicrobial peptides) have emerged from their origins as nature's antibiotics and are widely distributed in organisms from insects to plants to mammals and non-mammalian vertebrates. Although their original and primary function was proposed to be direct antimicrobial activity against bacteria, fungi, parasites and/or viruses, cationic HDPs are becoming increasingly recognized as multifunctional mediators, with both antimicrobial activity and diverse immunomodulatory properties. Here we provide an overview of the antimicrobial and immunomodulatory activities of cationic HDPs, and discuss their potential application as beneficial therapeutics in overcoming infectious diseases.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Antibiotics (Basel)
                Journal ID (iso-abbrev): Antibiotics (Basel)
                Journal ID (publisher-id): antibiotics
                Title: Antibiotics
                Publisher: MDPI
                ISSN (Electronic): 2079-6382
                Publication date (Electronic): 18 April 2019
                Publication date Collection: June 2019
                Volume: 8
                Issue: 2
                Electronic Location Identifier: 44
                Affiliations
                [1 ]School of Chemistry, University of New South Wales, Sydney, NSW 2052, Australia; r.kuppusamy@ 123456ad.unsw.edu.au (R.K.); d.black@ 123456unsw.edu.au (D.S.B.)
                [2 ]School of Optometry and Vision Science, University of New South Wales, Sydney, NSW 2052, Australia; m.willcox@ 123456unsw.edu.au
                Author notes
                [* ]Correspondence: n.kumar@ 123456unsw.edu.au ; Tel.: +61-293-854-698; Fax: +61-293-856-141
                Author information
                https://orcid.org/0000-0003-3842-7563
                Article
                Publisher ID: antibiotics-08-00044
                DOI: 10.3390/antibiotics8020044
                PMC ID: 6628222
                PubMed ID: 31003540
                SO-VID: 579d3290-e5ec-4886-b6d8-92e97f13be72
                Copyright © © 2019 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 29 March 2019
                Date accepted : 15 April 2019
                Categories
                Subject: Review

                Keywords: peptidomimetics,antibacterials,cationic groups
                Data availability:
                Keywords: peptidomimetics, antibacterials, cationic groups

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