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Antimicrobial Peptides as New Weapons to Fight Antimicrobial Resistance

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A special issue of Pharmaceuticals (ISSN 1424-8247). This special issue belongs to the section "Biopharmaceuticals".

Deadline for manuscript submissions: closed (1 December 2021) | Viewed by 12180

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Special Issue Editor

Dr. Angela Arciello

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Guest Editor

Department of Chemical Sciences, University of Naples Federico II, Via Cinthia 4, 80126 Naples, Italy
Interests: antimicrobial peptides; disease related proteins; antimicrobial resistance; food preservation; cosmeceutical formulations

Special Issue Information

Dear Colleagues,

It has been extensively reported that prolonged exposure to antibiotics is responsible for the development of multidrug resistant organisms (MDROs). Indeed, over the past four decades, there has been an explosion of so-called “superbugs”, such as vancomycin-resistant enterococci (VRE) and multidrug-resistant Pseudomonas, Klebsiella, and Acinetobacter bacterial strains. It is also known that microbes in a biofilm community gain additional antibiotic resistance that can be up to 1000 times higher than that gained by the corresponding planktonic cells. Therefore, the emergence of resistance to multiple antimicrobial agents has become a serious public health threat with great social and economic impacts. It should also be highlighted that the discovery, development, manufacture, and marketing of new antibiotics has significantly slowed down in the past 20 years. Thus, effective alternative strategies to conventional antibiotics are urgently needed. Consequently, naturally occurring host defence peptides (HDPs), first called antimicrobial peptides (AMPs), have attracted considerable attention because of their antimicrobial, anti-biofilm, and immunomodulatory properties but, above all, because they generally do not lead to selection of resistant strains, since this would require an almost complete remodeling of the bacterial membrane architecture. To date, over 1700 endogenous antimicrobial peptides have been isolated, with even more synthetic analogues reported in the literature. Because of their diverse spectrum of activity against microbial pathogens, both as innate defence molecules and as immunomodulators, HDPs are attractive candidates for the development of a new generation of antibiotics. This Special Issue has the aim of summarizing the state of the art and the latest findings published in the field of antimicrobial peptides, as well as elucidating future directions of research.

Dr. Angela Arciello
Guest Editor

Manuscript Submission Information

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Keywords

Antimicrobial peptides
Antimicrobial resistance
Peptide-based drugs
Antibiofilm peptides

Published Papers (4 papers)

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Research

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13 pages, 2193 KiB

Open AccessArticle

Production and Purification of Two Bioactive Antimicrobial Peptides Using a Two-Step Approach Involving an Elastin-Like Fusion Tag

by Ana Margarida Pereira, André da Costa, Simoni Campos Dias, Margarida Casal and Raul Machado

Pharmaceuticals 2021, 14(10), 956; https://0-doi-org.brum.beds.ac.uk/10.3390/ph14100956 - 23 Sep 2021

Cited by 11 | Viewed by 2905

Abstract

Antimicrobial resistance is an increasing global threat, demanding new therapeutic biomolecules against multidrug-resistant bacteria. Antimicrobial peptides (AMPs) are promising candidates for a new generation of antibiotics, but their potential application is still in its infancy, mostly due to limitations associated with large-scale production. The use of recombinant DNA technology for the production of AMPs fused with polymer tags presents the advantage of high-yield production and cost-efficient purification processes at high recovery rates. Owing to their unique properties, we explored the use of an elastin-like recombinamer (ELR) as a fusion partner for the production and isolation of two different AMPs (ABP-CM4 and Synoeca-MP), with an interspacing formic acid cleavage site. Recombinant AMP-ELR proteins were overproduced in Escherichia coli and efficiently purified by temperature cycles. The introduction of a formic acid cleavage site allowed the isolation of AMPs, resorting to a two-step methodology involving temperature cycles and a simple size-exclusion purification step. This simple and easy-to-implement purification method was demonstrated to result in high recovery rates of bioactive AMPs. The minimum inhibitory concentration (MIC) of the free AMPs was determined against seven different bacteria of clinical relevance (Staphylococcus aureus, Staphylococcus epidermidis, Escherichia coli, Klebsiella pneumoniae, Pseudomonas aeruginosa, and two Burkholderia cenocepacia strains), in accordance with the EUCAST/CLSI antimicrobial susceptibility testing standards. All the bacterial strains (except for Pseudomonas aeruginosa) were demonstrated to be susceptible to ABP-CM4, including a resistant Burkholderia cenocepacia clinical strain. As for Synoeca-MP, although it did not inhibit the growth of Pseudomonas aeruginosa or Klebsiella pneumoniae, it was demonstrated to be highly active against the remaining bacteria. The present work provides the basis for the development of an efficient and up-scalable biotechnological platform for the production and purification of active AMPs against clinically relevant bacteria. Full article

(This article belongs to the Special Issue Antimicrobial Peptides as New Weapons to Fight Antimicrobial Resistance)

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Graphical abstract

21 pages, 3126 KiB

Open AccessArticle

Impact of a Single Point Mutation on the Antimicrobial and Fibrillogenic Properties of Cryptides from Human Apolipoprotein B

by Rosa Gaglione, Giovanni Smaldone, Angela Cesaro, Mariano Rumolo, Maria De Luca, Rocco Di Girolamo, Luigi Petraccone, Pompea Del Vecchio, Rosario Oliva, Eugenio Notomista, Emilia Pedone and Angela Arciello

Pharmaceuticals 2021, 14(7), 631; https://0-doi-org.brum.beds.ac.uk/10.3390/ph14070631 - 29 Jun 2021

Cited by 12 | Viewed by 2379

Abstract

Host defense peptides (HDPs) are gaining increasing interest, since they are endowed with multiple activities, are often effective on multidrug resistant bacteria and do not generally lead to the development of resistance phenotypes. Cryptic HDPs have been recently identified in human apolipoprotein B and found to be endowed with a broad-spectrum antimicrobial activity, with anti-biofilm, wound healing and immunomodulatory properties, and with the ability to synergistically act in combination with conventional antibiotics, while being not toxic for eukaryotic cells. Here, a multidisciplinary approach was used, including time killing curves, differential scanning calorimetry, circular dichroism, ThT binding assays, and transmission electron microscopy analyses. The effects of a single point mutation (Pro → Ala in position 7) on the biological properties of ApoB-derived peptide r(P)ApoB_L^Pro have been evaluated. Although the two versions of the peptide share similar antimicrobial and anti-biofilm properties, only r(P)ApoB_L^Ala peptide was found to exert bactericidal effects. Interestingly, antimicrobial activity of both peptide versions appears to be dependent from their interaction with specific components of bacterial surfaces, such as LPS or LTA, which induce peptides to form β-sheet-rich amyloid-like structures. Altogether, obtained data indicate a correlation between ApoB-derived peptides self-assembling state and their antibacterial activity. Full article

(This article belongs to the Special Issue Antimicrobial Peptides as New Weapons to Fight Antimicrobial Resistance)

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Graphical abstract

16 pages, 9293 KiB

Open AccessArticle

Antimicrobial Peptides: Identification of two Beta-Defensins in a Teleost Fish, the European Sea Bass (Dicentrarchus labrax)

by Carolina Barroso, Pedro Carvalho, José F. M. Gonçalves, Pedro N. S. Rodrigues and João V. Neves

Pharmaceuticals 2021, 14(6), 566; https://0-doi-org.brum.beds.ac.uk/10.3390/ph14060566 - 14 Jun 2021

Cited by 9 | Viewed by 2770

Abstract

Beta-defensins consist in a group of cysteine-rich antimicrobial peptides (AMPs), widely found throughout vertebrate species, including teleost fish, with antimicrobial and immunomodulatory activities. However, although the European sea bass (Dicentrarchus labrax) is one of the most commercially important farmed fish species in the Mediterranean area, the characterization of its beta-defensins and its potential applications are still missing. In this study, we characterized two members of the beta-defensin family in this species. Phylogenetic and synteny analysis places sea bass peptides in the beta-defensin subfamilies 1 and 2, sharing similar features with the other members, including the six cysteines and the tertiary structure, that consists in three antiparallel beta-sheets, with beta-defensin 1 presenting an extra alpha-helix at the N-terminal. Further studies are necessary to uncover the functions of sea bass beta-defensins, particularly their antimicrobial and immunomodulatory properties, in order to develop novel prophylactic or therapeutic compounds to be used in aquaculture production. Full article

(This article belongs to the Special Issue Antimicrobial Peptides as New Weapons to Fight Antimicrobial Resistance)

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Review

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13 pages, 1571 KiB

Open AccessReview

Investigating Potential Applications of the Fish Anti-Microbial Peptide Pleurocidin: A Systematic Review

by Katelyn A. M. McMillan and Melanie R. Power Coombs

Pharmaceuticals 2021, 14(7), 687; https://0-doi-org.brum.beds.ac.uk/10.3390/ph14070687 - 17 Jul 2021

Cited by 6 | Viewed by 3029

Abstract

The anti-microbial peptide (AMP) pleurocidin is found in winter flounder (Pseudopleuronectes americanus), an Atlantic flounder species. There is promising evidence for clinical, aquaculture, and veterinary applications of pleurocidin. This review provides an overview of the current literature available on pleurocidin to guide future research directions. By fully elucidating pleurocidin’s mechanism of action and developing novel treatments against pathogenic microbes, populations of flatfish and humans can be protected. This review consulted publications from PubMed and Environment Complete with search terms such as “pleurocidin”, “winter flounder”, and “antimicrobial”. The fish immune system includes AMPs as a component of the innate immune system. Pleurocidin, one of these AMPs, has been found to be effective against various Gram-positive and Gram-negative bacteria. More investigations are required to determine pleurocidin’s suitability as a treatment against antibiotic-resistant pathogens. There is promising evidence for pleurocidin as a novel anti-cancer therapy. The peptide has been found to display potent anti-cancer effects against human cancer cells. Research efforts focused on pleurocidin may result in novel treatment strategies against antibiotic-resistant bacteria and cancer. More research is required to determine if the peptide is a suitable candidate to be developed into a novel anti-microbial treatment. Some of the microbes susceptible to the peptide are also pathogens of fish, suggesting its suitability as a therapeutic treatment for fish species. Full article

(This article belongs to the Special Issue Antimicrobial Peptides as New Weapons to Fight Antimicrobial Resistance)

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