Special Issue "Antimicrobial Peptides, Polymers and Surfaces"

A special issue of Antibiotics (ISSN 2079-6382). This special issue belongs to the section "Antimicrobial Peptides".

Deadline for manuscript submissions: closed (31 October 2019).

Special Issue Editor

Dr. Gregory Caputo
E-Mail Website1 Website2
Guest Editor
Department of Chemistry and Biochemistry, Rowan University, Glassboro, NJ 08028, USA
Interests: antimicrobial peptides; antimicrobial surfaces; peptide-lipid interactions; spectroscopy; fluorescence; circular dichroism; thin films

Special Issue Information

Dear Colleagues,

The development of antibiotic resistance in bacteria is a major public health threat facing the world today. The fight against antibiotic resistance requires a multidimensional approach to develop novel antimicrobials, novel methods of delivery for antibiotics, and novel materials to resist bacterial contamination. This Special Issue is aimed at highlighting ongoing and emerging research in the areas of antimicrobial peptides, antimicrobial polymers, and antimicrobial surfaces. These areas comprise a tremendous variety of research directed at developing novel compounds for treating infections and the development of novel materials to prevent contamination and spread of bacteria. These areas are inherently interconnected as lessons from one are often applied to others. The issue is open to research from synthesis to materials characterization to biochemical/biophysical characterization of mechanism of action.

Dr. Gregory Caputo
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. Antibiotics 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

  • antibacterial materials
  • antimicrobial peptides
  • antimicrobial polymers
  • thin films
  • materials
  • biofilms
  • antifungal

Published Papers (3 papers)

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Article
Characterization and Antimicrobial Activity of Amphiphilic Peptide AP3 and Derivative Sequences
Antibiotics 2019, 8(1), 20; https://0-doi-org.brum.beds.ac.uk/10.3390/antibiotics8010020 - 06 Mar 2019
Cited by 9 | Viewed by 1646
Abstract
The continued emergence of new antibiotic resistant bacterial strains has resulted in great interest in the development of new antimicrobial treatments. Antimicrobial peptides (AMPs) are one of many potential classes of molecules to help meet this emerging need. AMPs are naturally derived sequences, [...] Read more.
The continued emergence of new antibiotic resistant bacterial strains has resulted in great interest in the development of new antimicrobial treatments. Antimicrobial peptides (AMPs) are one of many potential classes of molecules to help meet this emerging need. AMPs are naturally derived sequences, which act as part of the innate immune system of organisms ranging from insects through humans. We investigated the antimicrobial peptide AP3, which is originally isolated from the winter flounder Pleuronectes americanus. This peptide is of specific interest because it does not exhibit the canonical facially amphiphilic orientation of side chains when in a helical orientation. Different analogs of AP3 were synthesized in which length, charge identity, and Trp position were varied to investigate the sequence-structure and activity relationship. We performed biophysical and microbiological characterization using fluorescence spectroscopy, CD spectroscopy, vesicle leakage assays, bacterial membrane permeabilization assays, and minimal inhibitory concentration (MIC) assays. Fluorescence spectroscopy showed that the peptides bind to lipid bilayers to similar extents, while CD spectra show the peptides adopt helical conformations. All five peptides tested in this study exhibited binding to model lipid membranes, while the truncated peptides showed no measurable antimicrobial activity. The most active peptide proved to be the parent peptide AP3 with the highest degree of leakage and bacterial membrane permeabilization. Moreover, it was found that the ability to permeabilize model and bacterial membranes correlated most closely with the ability to predict antimicrobial activity. Full article
(This article belongs to the Special Issue Antimicrobial Peptides, Polymers and Surfaces)
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Article
Solution-Mediated Modulation of Pseudomonas aeruginosa Biofilm Formation by a Cationic Synthetic Polymer
Antibiotics 2019, 8(2), 61; https://0-doi-org.brum.beds.ac.uk/10.3390/antibiotics8020061 - 10 May 2019
Cited by 4 | Viewed by 2644
Abstract
Bacterial biofilms and their associated infections are a continuing problem in the healthcare community. Previous approaches utilizing anti-biofilm coatings suffer from short lifetimes, and their applications are limited to surfaces. In this research, we explored a new approach to biofilm prevention based on [...] Read more.
Bacterial biofilms and their associated infections are a continuing problem in the healthcare community. Previous approaches utilizing anti-biofilm coatings suffer from short lifetimes, and their applications are limited to surfaces. In this research, we explored a new approach to biofilm prevention based on the hypothesis that changing planktonic bacteria behavior to result in sub-optimal biofilm formation. The behavior of planktonic Pseudomonas aeruginosa exposed to a cationic polymer was characterized for changes in growth behavior and aggregation behavior, and linked to resulting P. aeruginosa biofilm formation, biomass, viability, and metabolic activity. The incubation of P. aeruginosa planktonic bacteria with a cationic polymer resulted in the aggregation of planktonic bacteria, and a reduction in biofilm development. We propose that cationic polymers may sequester planktonic bacteria away from surfaces, thereby preventing their attachment and suppressing biofilm formation. Full article
(This article belongs to the Special Issue Antimicrobial Peptides, Polymers and Surfaces)
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Article
Pan-Drug Resistant Acinetobacter baumannii, but Not Other Strains, Are Resistant to the Bee Venom Peptide Melittin
Antibiotics 2020, 9(4), 178; https://0-doi-org.brum.beds.ac.uk/10.3390/antibiotics9040178 - 14 Apr 2020
Cited by 5 | Viewed by 1187
Abstract
Acinetobacter baumannii is a prevalent pathogen in hospital settings with increasing importance in infections associated with biofilm production. Due to a rapid increase in its drug resistance and the failure of commonly available antibiotics to treat A. baumannii infections, this bacterium has become [...] Read more.
Acinetobacter baumannii is a prevalent pathogen in hospital settings with increasing importance in infections associated with biofilm production. Due to a rapid increase in its drug resistance and the failure of commonly available antibiotics to treat A. baumannii infections, this bacterium has become a critical public health issue. For these multi-drug resistant A. baumannii, polymyxin antibiotics are considered the only option for the treatment of severe infections. Concerning, several polymyxin-resistant A. baumannii strains have been isolated over the last few years. This study utilized pan drug-resistant (PDR) strains of A. baumannii isolated in Brazil, along with susceptible (S) and extreme drug-resistant (XDR) strains in order to evaluate the in vitro activity of melittin, an antimicrobial peptide, in comparison to polymyxin and another antibiotic, imipenem. From a broth microdilution method, the determined minimum inhibitory concentration showed that S and XDR strains were susceptible to melittin. In contrast, PDR A. baumannii was resistant to all treatments. Treatment with the peptide was also observed to inhibit biofilm formation of a susceptible strain and appeared to cause permanent membrane damage. A subpopulation of PDR showed membrane damage, however, it was not sufficient to stop bacterial growth, suggesting that alterations involved with antibiotic resistance could also influence melittin resistance. Presumably, mutations in the PDR that have arisen to confer resistance to widely used therapeutics also confer resistance to melittin. Our results demonstrate the potential of melittin to be used in the control of bacterial infections and suggest that antimicrobial peptides can serve as the basis for the development of new treatments. Full article
(This article belongs to the Special Issue Antimicrobial Peptides, Polymers and Surfaces)
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