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Special Issue "Antimicrobial Peptides: From Synthesis to Application"

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

Deadline for manuscript submissions: 31 August 2020.

Special Issue Editor

Dr. Vincent Humblot
Website
Guest Editor
Laboratoire de Réactivité de Surface UMR CNRS 7197, Sorbonne Université, Paris, France
Interests: self-assembled monolayers, surface modification, grafted anti-microbial peptides, bacterial biofilms, antibacterial surfaces, peptides modifications, peptides chirality

Special Issue Information

Dear Colleagues,

Bacterial resistance to current antibiotic treatments is a growing cause for concern. Nosocomial and medical device-induced biofilm infections affect millions of lives and urgently require novel therapeutic approaches to overcome this alarming issue. Development of new antimicrobial strategies is an emergent topic and both natural and synthetic propositions are currently under testing for clinical approval and use. Among those, antimicrobial peptides (AMPs) make promising candidates to prevent bacterial infection. Over the past few decades, antimicrobial peptides have yielded fascinating research and perspectives due to the huge number of natural peptides that can be found in nature.

This Special Issue of Molecules will be devoted to the molecular and structural diversity of AMPs with a focus on genome-mining approaches to explore the biodiversity of AMP sequences. It will also cover different functional aspects, such as mechanism of action, molecular evolution, acquisition of multiple functions, and surface functionalization with AMPs to fight biofilm formation or as carrier agents. The application field will be covered through the interactions between antimicrobial peptides and microbiotas or resistance to antimicrobial peptides and their therapeutic applications.

Dr. Vincent Humblot
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 semimonthly 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 2000 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

  • antimicrobial peptides
  • diversity (origins, structures, and biological activities)
  • multifunction
  • resistance
  • vectorization and formulation
  • microbial ecology
  • microbial resistance
  • valorization
  • surface functionalization

Published Papers (3 papers)

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Research

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Open AccessArticle
Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18
Molecules 2020, 25(3), 485; https://doi.org/10.3390/molecules25030485 - 23 Jan 2020
Cited by 1
Abstract
Pantoea dispersa W18, isolated from contaminated soil, was found to exert antimicrobial activity against Mycobacterium species, including Mycobacterium tuberculosis, an important human pathogen. Here, the anti-mycobacterial compound produced by Pantoea dispersa W18 was purified by a combination of hydrophobic interaction chromatography, cation [...] Read more.
Pantoea dispersa W18, isolated from contaminated soil, was found to exert antimicrobial activity against Mycobacterium species, including Mycobacterium tuberculosis, an important human pathogen. Here, the anti-mycobacterial compound produced by Pantoea dispersa W18 was purified by a combination of hydrophobic interaction chromatography, cation exchange chromatography, and reverse phase HPLC. Active compounds from Pantoea dispersa W18 were identified as a natural peptide named pantocin wh-1 with a 1927 Da molecular weight. The primary structure of this compound was detected by N-terminal amino acid sequencing. The amino acid sequence of pantocin wh-1 consisted of 16 amino acid residues with a cyclic structure. The pantocin wh-1 could be inactivated by protease K, but was heat stable and unaffected by pH (2–12). However, the activity was not completely inactivated by trypsin and pepsin. This is the first report of a cyclic polypeptide purified from a strain of Pantoea dispersa. Full article
(This article belongs to the Special Issue Antimicrobial Peptides: From Synthesis to Application)
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Open AccessArticle
Structure-Activity Study of an All-d Antimicrobial Octapeptide D2D
Molecules 2019, 24(24), 4571; https://doi.org/10.3390/molecules24244571 - 13 Dec 2019
Abstract
The increasing emergence of multi-drug resistant bacteria is a serious threat to public health worldwide. Antimicrobial peptides have attracted attention as potential antibiotics since they are present in all multicellular organisms and act as a first line of defence against invading pathogens. We [...] Read more.
The increasing emergence of multi-drug resistant bacteria is a serious threat to public health worldwide. Antimicrobial peptides have attracted attention as potential antibiotics since they are present in all multicellular organisms and act as a first line of defence against invading pathogens. We have previously identified a small all-d antimicrobial octapeptide amide kk(1-nal)fk(1-nal)k(nle)-NH2 (D2D) with promising antimicrobial activity. In this work, we have performed a structure-activity relationship study of D2D based on 36 analogues aimed at discovering which elements are important for antimicrobial activity and toxicity. These modifications include an alanine scan, probing variation of hydrophobicity at lys5 and lys7, manipulation of amphipathicity, N-and C-termini deletions and lys-arg substitutions. We found that the hydrophobic residues in position 3 (1-nal), 4 (phe), 6 (1-nal) and 8 (nle) are important for antimicrobial activity and to a lesser extent cationic lysine residues in position 1, 2, 5 and 7. Our best analogue 5, showed MICs of 4 µg/mL against A. baumannii, E. coli, P. aeruginosa and S. aureus with a hemolytic activity of 47% against red blood cells. Furthermore, compound 5 kills bacteria in a concentration-dependent manner as shown by time-kill kinetics. Circular dichroism (CD) spectra of D2D and compounds 18 showed that they likely fold into α-helical secondary structure. Small angle x-ray scattering (SAXS) experiments showed that a random unstructured polymer-like chains model could explain D2D and compounds 1, 3, 4, 6 and 8. Solution structure of compound 5 can be described with a nanotube structure model, compound 7 can be described with a filament-like structure model, while compound 2 can be described with both models. Lipid interaction probed by small angle X-ray scattering (SAXS) showed that a higher amount of compound 5 (~50–60%) inserts into the bilayer compared to D2D (~30–50%). D2D still remains the lead compound, however compound 5 is an interesting antimicrobial peptide for further investigations due to its nanotube structure and minor improvement to antimicrobial activity compared to D2D. Full article
(This article belongs to the Special Issue Antimicrobial Peptides: From Synthesis to Application)
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Review

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Open AccessReview
Antimicrobial Peptides as Probes in Biosensors Detecting Whole Bacteria: A Review
Molecules 2020, 25(8), 1998; https://doi.org/10.3390/molecules25081998 - 24 Apr 2020
Abstract
Bacterial resistance is becoming a global issue due to its rapid growth. Potential new drugs as antimicrobial peptides (AMPs) are considered for several decades as promising candidates to circumvent this threat. Nonetheless, AMPs have also been used more recently in other settings such [...] Read more.
Bacterial resistance is becoming a global issue due to its rapid growth. Potential new drugs as antimicrobial peptides (AMPs) are considered for several decades as promising candidates to circumvent this threat. Nonetheless, AMPs have also been used more recently in other settings such as molecular probes grafted on biosensors able to detect whole bacteria. Rapid, reliable and cost-efficient diagnostic tools for bacterial infection could prevent the spread of the pathogen from the earliest stages. Biosensors based on AMPs would enable easy monitoring of potentially infected samples, thanks to their powerful versatility and integrability in pre-existent settings. AMPs, which show a broad spectrum of interactions with bacterial membranes, can be tailored in order to design ubiquitous biosensors easily adaptable to clinical settings. This review aims to focus on the state of the art of AMPs used as the recognition elements of whole bacteria in label-free biosensors with a particular focus on the characteristics obtained in terms of threshold, volume of sample analysable and medium, in order to assess their workability in real-world applications. Full article
(This article belongs to the Special Issue Antimicrobial Peptides: From Synthesis to Application)
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