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      Activity of Anti-Microbial Peptides (AMPs) against Leishmania and Other Parasites: An Overview

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          Abstract

          Anti-microbial peptides (AMPs), small biologically active molecules, produced by different organisms through their innate immune system, have become a considerable subject of interest in the request of novel therapeutics. Most of these peptides are cationic-amphipathic, exhibiting two main mechanisms of action, direct lysis and by modulating the immunity. The most commonly reported activity of AMPs is their anti-bacterial effects, although other effects, such as anti-fungal, anti-viral, and anti-parasitic, as well as anti-tumor mechanisms of action have also been described. Their anti-parasitic effect against leishmaniasis has been studied. Leishmaniasis is a neglected tropical disease. Currently among parasitic diseases, it is the second most threating illness after malaria. Clinical treatments, mainly antimonial derivatives, are related to drug resistance and some undesirable effects. Therefore, the development of new therapeutic agents has become a priority, and AMPs constitute a promising alternative. In this work, we describe the principal families of AMPs (melittin, cecropin, cathelicidin, defensin, magainin, temporin, dermaseptin, eumenitin, and histatin) exhibiting a potential anti-leishmanial activity, as well as their effectiveness against other microorganisms.

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          Antimicrobial peptides of multicellular organisms.

          Multicellular organisms live, by and large, harmoniously with microbes. The cornea of the eye of an animal is almost always free of signs of infection. The insect flourishes without lymphocytes or antibodies. A plant seed germinates successfully in the midst of soil microbes. How is this accomplished? Both animals and plants possess potent, broad-spectrum antimicrobial peptides, which they use to fend off a wide range of microbes, including bacteria, fungi, viruses and protozoa. What sorts of molecules are they? How are they employed by animals in their defence? As our need for new antibiotics becomes more pressing, could we design anti-infective drugs based on the design principles these molecules teach us?
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            APD3: the antimicrobial peptide database as a tool for research and education

            The antimicrobial peptide database (APD, http://aps.unmc.edu/AP/) is an original database initially online in 2003. The APD2 (2009 version) has been regularly updated and further expanded into the APD3. This database currently focuses on natural antimicrobial peptides (AMPs) with defined sequence and activity. It includes a total of 2619 AMPs with 261 bacteriocins from bacteria, 4 AMPs from archaea, 7 from protists, 13 from fungi, 321 from plants and 1972 animal host defense peptides. The APD3 contains 2169 antibacterial, 172 antiviral, 105 anti-HIV, 959 antifungal, 80 antiparasitic and 185 anticancer peptides. Newly annotated are AMPs with antibiofilm, antimalarial, anti-protist, insecticidal, spermicidal, chemotactic, wound healing, antioxidant and protease inhibiting properties. We also describe other searchable annotations, including target pathogens, molecule-binding partners, post-translational modifications and animal models. Amino acid profiles or signatures of natural AMPs are important for peptide classification, prediction and design. Finally, we summarize various database applications in research and education.
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              Antimicrobial Peptides

              The rapid increase in drug-resistant infections has presented a serious challenge to antimicrobial therapies. The failure of the most potent antibiotics to kill “superbugs” emphasizes the urgent need to develop other control agents. Here we review the history and new development of antimicrobial peptides (AMPs), a growing class of natural and synthetic peptides with a wide spectrum of targets including viruses, bacteria, fungi, and parasites. We summarize the major types of AMPs, their modes of action, and the common mechanisms of AMP resistance. In addition, we discuss the principles for designing effective AMPs and the potential of using AMPs to control biofilms (multicellular structures of bacteria embedded in extracellular matrixes) and persister cells (dormant phenotypic variants of bacterial cells that are highly tolerant to antibiotics).
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                Author and article information

                Contributors
                Role: Academic Editor
                Journal
                Biomolecules
                Biomolecules
                biomolecules
                Biomolecules
                MDPI
                2218-273X
                04 July 2021
                July 2021
                : 11
                : 7
                : 984
                Affiliations
                [1 ]ISTUN Instituto de Salud Tropical, Department of Microbiology and Parasitology, IdiSNA (Navarra Institute for Health Research), University of Navarra, c/Irunlarrea 1, 31008 Pamplona, Navarra, Spain; reldirany@ 123456alumni.unav.es
                [2 ]Faculty of Sciences I, Lebanese University, Hadath 1003, Lebanon; hshahrour@ 123456alumni.unav.es (H.S.); fabdelsa@ 123456ul.edu.lb (F.A.-S.)
                [3 ]Department of Microbiology and Parasitology, IdiSNA (Navarra Institute for Health Research), University of Navarra, 31008 Pamplona, Navarra, Spain; gmartinez@ 123456unav.es
                [4 ]Department of Chemistry, Faculty of Sciences, University of Navarra, 31080 Pamplona, Navarra, Spain; zdiranyahma@ 123456alumni.unav.es (Z.D.); gaitano@ 123456unav.es (G.G.-G.)
                [5 ]Brandenburg Antiinfektiva GmbH, c/o Forschungszentrum Borstel, Leibniz Lungenzentrum, 23845 Borstel, Germany; kbranden@ 123456gmx.de
                Author notes
                [* ]Correspondence: panguewa@ 123456unav.es
                [†]

                These authors contributed equally to this work.

                Author information
                https://orcid.org/0000-0002-4787-8262
                https://orcid.org/0000-0002-1477-6710
                https://orcid.org/0000-0003-3755-451X
                https://orcid.org/0000-0002-2193-7316
                Article
                biomolecules-11-00984
                10.3390/biom11070984
                8301979
                fef0b9fc-d9ba-45b4-8f35-a65c457c80c4
                © 2021 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 (CC BY) license ( https://creativecommons.org/licenses/by/4.0/).

                History
                : 22 May 2021
                : 26 June 2021
                Categories
                Review

                anti-microbial peptides (amps),anti-bacterial,anti-fungal,anti-viral,anti-parasitic,anti-tumor,leishmania,parasite,bacteria,cathelicidin,cecropin,defensin,dermaseptin,eumentin,histatin,magainin,melittin,temporin

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