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Special Issue "Antimicrobial Peptides and Peptidomimetics"

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: 20 January 2018

Special Issue Editor

Guest Editor
Assoc. Prof. Steven L Cobb

Department of Chemistry, Durham University, South Road, Durham, DH1 3LE, UK
Website | E-Mail
Interests: peptides; peptoids; infectious diseases; chemical-biology; organic synthesis

Special Issue Information

Dear Colleagues,

Our ability to treat what we currently consider minor bacterial infections underpins all of modern medicine and the future cost of failure to treat such infections is enormous both in terms of societal and economic impacts. The situation is exacerbated by the fact that the number of new antibiotics being brought to market is at an all-time low. There is an urgent need for new antibiotics that can be used to treat the rapid emergence of antimicrobial resistance.

The effectiveness of the innate immune system in providing the first line of defence against infection, has led main research groups around the world to investigate the activities of antimicrobial peptides (AMPs), with a view to their use as templates for the design of innovative therapeutics to combat emerging antimicrobial resistance. However, despite their considerable promise in terms of biological activity, efforts to develop AMPs as generic antibiotics have been hampered by their inherent chemical instability and susceptibility to enzymatic degradation. Only a handful of AMPs are currently in clinical trials.

This Special Issue is aimed at covering recent advances in the synthesis, mechanistic understanding and applications of antimicrobial peptides (and peptidomimetics) in the development of new agents for the treatment of microbial infections.  

Assoc. Prof. Steven L Cobb
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Microbial Infection (bacterial, fungal and parasitic)
  • Antimicrobial Peptides
  • Peptoids
  • Peptidomimetics
  • Synthesis
  • Mode of action
  • Structure and properties
  • Biophysics

Published Papers (3 papers)

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Research

Open AccessArticle Design, Recombinant Fusion Expression and Biological Evaluation of Vasoactive Intestinal Peptide Analogue as Novel Antimicrobial Agent
Molecules 2017, 22(11), 1963; doi:10.3390/molecules22111963
Received: 12 October 2017 / Accepted: 8 November 2017 / Published: 14 November 2017
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Abstract
Antimicrobial peptides represent an emerging category of therapeutic agents with remarkable structural and functional diversity. Modified vasoactive intestinal peptide (VIP) (VIP analogue 8 with amino acid sequence “FTANYTRLRRQLAVRRYLAAILGRR”) without haemolytic activity and cytotoxicity displayed enhanced antimicrobial activities against Staphylococcus aureus (S. aureus
[...] Read more.
Antimicrobial peptides represent an emerging category of therapeutic agents with remarkable structural and functional diversity. Modified vasoactive intestinal peptide (VIP) (VIP analogue 8 with amino acid sequence “FTANYTRLRRQLAVRRYLAAILGRR”) without haemolytic activity and cytotoxicity displayed enhanced antimicrobial activities against Staphylococcus aureus (S. aureus) ATCC 25923 and Escherichia coli (E. coli) ATCC 25922 than parent VIP even in the presence of 180 mM NaCl or 50 mM MgCl2, or in the range of pH 4–10. VIP analogue 8 was expressed as fusion protein thioredoxin (Trx)-VIP8 in E. coli BL21(DE) at a yield of 45.67 mg/L. The minimum inhibitory concentration (MIC) of the recombinant VIP analogue 8 against S. aureus ATCC 25923 and E. coli ATCC 25922 were 2 μM. These findings suggest that VIP analogue 8 is a promising candidate for application as a new and safe antimicrobial agent. Full article
(This article belongs to the Special Issue Antimicrobial Peptides and Peptidomimetics)
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Open AccessArticle PSN-PC: A Novel Antimicrobial and Anti-Biofilm Peptide from the Skin Secretion of Phyllomedusa-camba with Cytotoxicity on Human Lung Cancer Cell
Molecules 2017, 22(11), 1896; doi:10.3390/molecules22111896
Received: 17 October 2017 / Revised: 30 October 2017 / Accepted: 2 November 2017 / Published: 7 November 2017
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Abstract
Peptides derived from amphibian skin secretion are promising drug prototypes for combating widespread infection. In this study, a novel peptide belonging to the phylloseptin family of antimicrobial peptides was isolated from the skin secretion of the Phyllomedusa camba, namely phylloseptin-PC (PSN-PC). The
[...] Read more.
Peptides derived from amphibian skin secretion are promising drug prototypes for combating widespread infection. In this study, a novel peptide belonging to the phylloseptin family of antimicrobial peptides was isolated from the skin secretion of the Phyllomedusa camba, namely phylloseptin-PC (PSN-PC). The biosynthetic precursor was obtained by molecular cloning and the mature peptide sequence was confirmed through tandem mass spectrometry (MS/MS) fragmentation sequencing in the skin secretion. The synthetic replicate exhibited a broad spectrum antimicrobial activity against Staphylococcus aureus, methicillin-resistant Staphylococcus aureus, Escherichia coli, Pseudomonas aeruginosa, Candida albicans at concentrations of 2, 2, 8, 32 and 2 µM, respectively. It also showed the capability of eliminating S. aureus biofilm with a minimal biofilm eradication concentration of 8 µM. The haemolysis of this peptide was not significant at low concentrations but had a considerable increase at high concentrations. Additionally, this peptide showed an anti-proliferation effect on the non-small cell lung cancer cell line (NCI-H157), with low cytotoxicity on the human microvascular endothelial cell line (HMEC-1). The discovery of the novel peptide may provide useful clues for new drug discoveries. Full article
(This article belongs to the Special Issue Antimicrobial Peptides and Peptidomimetics)
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Open AccessArticle Tryptophan-Containing Cyclic Decapeptides with Activity against Plant Pathogenic Bacteria
Molecules 2017, 22(11), 1817; doi:10.3390/molecules22111817
Received: 2 October 2017 / Revised: 25 October 2017 / Accepted: 25 October 2017 / Published: 26 October 2017
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Abstract
A library of 66 cyclic decapeptides incorporating a Trp residue was synthesized on solid phase and screened against the phytopathogenic bacteria Pseudomonas syringae pv. syringae, Xanthomonas axonopodis pv. vesicatoria, and Erwinia amylovora. The hemolytic activity of these peptides was also evaluated.
[...] Read more.
A library of 66 cyclic decapeptides incorporating a Trp residue was synthesized on solid phase and screened against the phytopathogenic bacteria Pseudomonas syringae pv. syringae, Xanthomonas axonopodis pv. vesicatoria, and Erwinia amylovora. The hemolytic activity of these peptides was also evaluated. The results obtained were compared with those of a collection of Phe analogues previously reported. The analysis of the data showed that the presence of the Trp improved the antibacterial activity against these three pathogens. In particular, 40 to 46 Trp analogues displayed lower minimum inhibitory concentration (MIC) values than their corresponding Phe counterparts. Interestingly, 26 Trp-containing sequences exhibited MIC of 0.8 to 3.1 μM against X. axonopodis pv. vesicatoria, 21 peptides MIC of 1.6 to 6.2 μM against P. syringae pv. syringae and six peptides MIC of 6.2 to 12.5 μM against E. amylovora. Regarding the hemolysis, in general, Trp derivatives displayed a percentage of hemolysis comparable to that of their Phe analogues. Notably, 49 Trp-containing cyclic peptides showed a hemolysis ≤ 20% at 125 μM. The peptides with the best biological activity profile were c(LKKKLWKKLQ) (BPC086W) and c(LKKKKWLLKQ) (BPC108W), which displayed MIC values ranging from 0.8 to 12.5 μM and a hemolysis ≤ 8% at 125 μM. Therefore, it is evident that these Trp sequences constitute promising candidates for the development of new agents for use in plant protection. Full article
(This article belongs to the Special Issue Antimicrobial Peptides and Peptidomimetics)
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