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      Antimicrobial peptides – Advances in development of therapeutic applications

      review-article
      Author(s): a , b , a , b , a , c , *
      Publication date (Electronic):
      Journal: Life Sciences
      Publisher: Published by Elsevier Inc.
      Keywords: AMPs, antimicrobial peptides, BAI, biomaterial-associated infection, BLES, bovine lipid extract surfactant, BMP, bone morphogenetic protein, CARG, compounded annual growth rate, CF, cystic fibrosis, CL, contact lens, COPD, chronic obstructive pulmonary disease, CRAMP, cathelin-related antimicrobial peptides, FCS, fetal calf serum, FDA, Food and Drug Administration, GI tract, gastrointestinal tract, HBD-1, human beta-defensin-1, HIV, human immunodeficiency viruses, LPS, lipopolysaccharides, LTA, lipoteichoic acid, MDR, MULTIDRUG RESIStant, MIC, minimum inhibitory concentration, PAMPs, pathogen-associated molecular patterns, PLGA, poly(lactic-co-glycolic acid), PS, phospholipid phosphatidylserine, RCM, ring-closing metathesis, ROS, reactive oxygen species, SDF, silver diamine flouride, SNPs, single-nucleotide polymorphisms, SSTIs, skin and soft tissue infections, STAMP, specifically targeted antimicrobial peptide, TKR, total hip and knee replacement, TNF, tumor necrosis factor, TRAIL, TNF-related apoptosis inducing ligand, Antimicrobial peptides (AMPs), Antimicrobial resistance, Infectious diseases, Anticancer agent, Medical devices, Cosmetic ingredients, Peptide drugs

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          Abstract

          The severe infection is becoming a significant health problem which threaten the lives of patients and the safety and economy of society. In the way of finding new strategy, antimicrobial peptides (AMPs) - an important part of host defense family, emerged with tremendous potential. Up to date, huge numbers of AMPs has been investigated from both natural and synthetic sources showing not only the ability to kill microbial pathogens but also propose other benefits such as wound healing, anti-tumor, immune modulation. In this review, we describe the involvements of AMPs in biological systems and discuss the opportunity in developing AMPs for clinical applications. In the detail, their properties in antibacterial activity is followed by their application in some infection diseases and cancer. The key discussions are the approaches to improve biological activities of AMPs either by modifying chemical structure or incorporating into delivery systems. The new applications and perspectives for the future of AMPs would open the new era of their development.

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          APD3: the antimicrobial peptide database as a tool for research and education

          Guangshun Wang, Xia Li, Zhe Wang (2015)
          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.
          Article 0 comments Cited 465 times – based on 0 reviews     Review now
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            The expanding scope of antimicrobial peptide structures and their modes of action.

            Leonard T. Nguyen, Evan Haney, Hans Vogel (2011)
            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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              Barrier properties of mucus.

              Richard Cone (2009)
              Mucus is tenacious. It sticks to most particles, preventing their penetration to the epithelial surface. Multiple low-affinity hydrophobic interactions play a major role in these adhesive interactions. Mucus gel is also shear-thinning, making it an excellent lubricant that ensures an unstirred layer of mucus remains adherent to the epithelial surface. Thus nanoparticles (NP) must diffuse readily through the unstirred adherent layer if they are to contact epithelial cells efficiently. This article reviews some of the physiological and biochemical properties that form the mucus barrier. Capsid viruses can diffuse through mucus as rapidly as through water and thereby penetrate to the epithelium even though they have to diffuse 'upstream' through mucus that is being continuously secreted. These viruses are smaller than the mucus mesh spacing, and have surfaces that do not stick to mucus. They form a useful model for developing NP for mucosal drug delivery.
              Article 0 comments Cited 304 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): Life Sci
                Journal ID (iso-abbrev): Life Sci
                Title: Life Sciences
                Publisher: Published by Elsevier Inc.
                ISSN (Print): 0024-3205
                ISSN (Electronic): 1879-0631
                Publication date PMC-release: 12 September 2020
                Publication date (Electronic): 12 September 2020
                Electronic Location Identifier: 118407
                Affiliations
                [a ]Faculty of Pharmacy, PHENIKAA University, Yen Nghia, Ha Dong, Hanoi 12116, Viet Nam
                [b ]PHENIKAA Institute for Advanced Study (PIAS), PHENIKAA University, Hanoi 12116, Viet Nam
                [c ]PHENIKAA Research and Technology Institute (PRATI), A&A Green Phoenix Group JSC, No.167 Hoang Ngan, Trung Hoa, Cau Giay, Hanoi 11313, Viet Nam
                Author notes
                [* ]Corresponding author at: Faculty of Pharmacy, PHENIKAA University, Yen Nghia, Ha Dong, Hanoi 12116, Viet Nam.
                Article
                Publisher ID: S0024-3205(20)31160-7 Publisher ID: 118407
                DOI: 10.1016/j.lfs.2020.118407
                PMC ID: 7486823
                PubMed ID: 32931796
                SO-VID: 3455821e-3af6-4799-8a07-818dbd0d94c2
                Copyright © © 2020 Published by Elsevier Inc.
                License:

                Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.

                History
                Date received : 26 June 2020
                Date revision received : 2 September 2020
                Date accepted : 7 September 2020
                Categories
                Subject: Article

                Keywords: amps, antimicrobial peptides,bai, biomaterial-associated infection,bles, bovine lipid extract surfactant,bmp, bone morphogenetic protein,carg, compounded annual growth rate,cf, cystic fibrosis,cl, contact lens,copd, chronic obstructive pulmonary disease,cramp, cathelin-related antimicrobial peptides,fcs, fetal calf serum,fda, food and drug administration,gi tract, gastrointestinal tract,hbd-1, human beta-defensin-1,hiv, human immunodeficiency viruses,lps, lipopolysaccharides,lta, lipoteichoic acid,mdr, multidrug resistant,mic, minimum inhibitory concentration,pamps, pathogen-associated molecular patterns,plga, poly(lactic-co-glycolic acid),ps, phospholipid phosphatidylserine,rcm, ring-closing metathesis,ros, reactive oxygen species,sdf, silver diamine flouride,snps, single-nucleotide polymorphisms,sstis, skin and soft tissue infections,stamp, specifically targeted antimicrobial peptide,tkr, total hip and knee replacement,tnf, tumor necrosis factor,trail, tnf-related apoptosis inducing ligand,antimicrobial peptides (amps),antimicrobial resistance,infectious diseases,anticancer agent,medical devices,cosmetic ingredients,peptide drugs
                Data availability:
                Keywords: amps, antimicrobial peptides, bai, biomaterial-associated infection, bles, bovine lipid extract surfactant, bmp, bone morphogenetic protein, carg, compounded annual growth rate, cf, cystic fibrosis, cl, contact lens, copd, chronic obstructive pulmonary disease, cramp, cathelin-related antimicrobial peptides, fcs, fetal calf serum, fda, food and drug administration, gi tract, gastrointestinal tract, hbd-1, human beta-defensin-1, hiv, human immunodeficiency viruses, lps, lipopolysaccharides, lta, lipoteichoic acid, mdr, multidrug resistant, mic, minimum inhibitory concentration, pamps, pathogen-associated molecular patterns, plga, poly(lactic-co-glycolic acid), ps, phospholipid phosphatidylserine, rcm, ring-closing metathesis, ros, reactive oxygen species, sdf, silver diamine flouride, snps, single-nucleotide polymorphisms, sstis, skin and soft tissue infections, stamp, specifically targeted antimicrobial peptide, tkr, total hip and knee replacement, tnf, tumor necrosis factor, trail, tnf-related apoptosis inducing ligand, antimicrobial peptides (amps), antimicrobial resistance, infectious diseases, anticancer agent, medical devices, cosmetic ingredients, peptide drugs

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