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Editorial Board Members' Collection Series: Structural Aspects of AMPs and Antimicrobials

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

Deadline for manuscript submissions: 31 July 2024 | Viewed by 10601

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Special Issue Editors

Prof. Dr. J. Michael Conlon

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Guest Editor

Diabetes Research Group, School of Biomedical Sciences, Ulster University, Coleraine BT52 1SA, N. Ireland, UK
Interests: naturally occurring antimicrobial peptides; drug discovery

Dr. Marc Maresca

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Guest Editor

CNRS, Aix-Marseille University, Centrale Marseille, iSm2, 13013 Marseille, France
Interests: mycotoxins; fungal metabolites; antimicrobial; anticancer; antinflammatory; antioxidant
Special Issues, Collections and Topics in MDPI journals

Prof. Dr. Bong-Jin Lee

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Guest Editor

The Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Gwanak-Gu, Seoul, Republic of Korea
Interests: peptide drug; antimicrobial peptide; structural study on antibiotic target proteins; toxin-antitoxin systems
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

We are pleased to announce this Special Issue, titled “Editorial Board Members' Collection Series: Structural aspects of AMPs and antimicrobials”. This issue is dedicated to collecting papers from the Editorial Board Members. In the context of the rising global incidence of antibiotic resistance, antimicrobial peptides (AMPs), peptidomimetics and polymers have been proposed as realistic alternatives to conventional antibiotics. Conventional antibiotics target enzymes and proteins with resistance frequently arising from structural mutations. In contrast, antimicrobial peptides/peptidomimetics/polymers by virtue of their different targets (for example the bacterial membrane or nucleic acids) are active on antibiotic-resistant strains and are less likely to produce resistance. In addition, antimicrobial peptides/peptidomimetics/polymers are multifunctional and may possess additional activities such as wound healing, anti-inflammatory, antifungal, antiviral, antitumoral or antibiofilm properties and may act synergistically with conventional antibiotics. The aim of this Special Issue is to provide a venue for networking and communication between Antibiotics and scholars in the field of structural aspects of antimicrobial peptides. Topics of interest include, but are not limited to, the following:

Diversity of origin of antimicrobial agents (natural peptides, ribosomally produced, ribosomally synthesized and posttranslationally modified peptides non-ribosomally produced peptides), synthetic peptides, peptidomimetics, antimicrobial polymers)
Diversity of conformation of antimicrobial peptides, peptidomimetics and polymers (helical, beta sheet, beta hairpin etc)
Diversity of activity of antimicrobial peptides, peptidomimetics and polymers (antibacterial, antifungal, antiviral, antitumoral, anti-inflammatory, antibiofilm, wound healing, synergy with antibiotics)
Peptidase-resistance
Host-defense, Innate immunity
Cytotoxicity
Bacterial antitoxins; Toxin-antitoxin complex; Antitoxin inhibition
Allostery
Circular Dichroism
NMR

Prof. Dr. J. Michael Conlon
Dr. Marc Maresca
Prof. Dr. Bong-Jin Lee
Guest Editors

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 submissions that pass pre-check are 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 2900 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.

Published Papers (7 papers)

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Research

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25 pages, 10225 KiB

Open AccessArticle

The Synthetic Peptide LyeTx I mn∆K, Derived from Lycosa erythrognatha Spider Toxin, Is Active against Methicillin-Resistant Staphylococcus aureus (MRSA) In Vitro and In Vivo

by Ana Paula Gonçalves Coelho Vieira, Amanda Neves de Souza, William Gustavo Lima, Julio Cesar Moreira Brito, Daniela Carolina Simião, Lucas Vinícius Ribeiro Gonçalves, Lídia Pereira Barbosa Cordeiro, Denise de Oliveira Scoaris, Simone Odília Antunes Fernandes, Jarbas Magalhães Resende, Burkhard Bechinger, Rodrigo Moreira Verly and Maria Elena de Lima

Antibiotics 2024, 13(3), 248; https://0-doi-org.brum.beds.ac.uk/10.3390/antibiotics13030248 - 08 Mar 2024

Viewed by 1130

Abstract

The urgent global health challenge posed by methicillin-resistant Staphylococcus aureus (MRSA) infections demands effective solutions. Antimicrobial peptides (AMPs) represent promising tools of research of new antibacterial agents and LyeTx I mn∆K, a short synthetic peptide based on the Lycosa erythrognatha spider venom, is a good representative. This study focused on analyzing the antimicrobial activities of LyeTx I mn∆K, including minimum inhibitory and bactericidal concentrations, synergy and resensitization assays, lysis activity, the effect on biofilm, and the bacterial death curve in MRSA. Additionally, its characterization was conducted through isothermal titration calorimetry, dynamic light scattering, calcein release, and finally, efficacy in a mice wound model. The peptide demonstrates remarkable efficacy against planktonic cells (MIC 8–16 µM) and biofilms (>30% of inhibition) of MRSA, and outperforms vancomycin in terms of rapid bactericidal action and anti-biofilm effects. The mechanism involves significant membrane damage. Interactions with bacterial model membranes, including those with lysylphosphatidylglycerol (LysylPOPG) modifications, highlight the versatility and selectivity of this compound. Also, the peptide has the ability to sensitize resistant bacteria to conventional antibiotics, showing potential for combinatory therapy. Furthermore, using an in vivo model, this study showed that a formulated gel containing the peptide proved superior to vancomycin in treating MRSA-induced wounds in mice. Together, the results highlight LyeTx I mnΔK as a promising prototype for the development of effective therapeutic strategies against superficial MRSA infections. Full article

(This article belongs to the Special Issue Editorial Board Members' Collection Series: Structural Aspects of AMPs and Antimicrobials)

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14 pages, 4286 KiB

Open AccessArticle

Antiviral Activity of Anthranilamide Peptidomimetics against Herpes Simplex Virus 1 and a Coronavirus

by Umme Laila Urmi, Samuel Attard, Ajay Kumar Vijay, Mark D. P. Willcox, Naresh Kumar, Salequl Islam and Rajesh Kuppusamy

Antibiotics 2023, 12(9), 1436; https://0-doi-org.brum.beds.ac.uk/10.3390/antibiotics12091436 - 12 Sep 2023

Viewed by 2045

Abstract

The development of potent antiviral agents is of utmost importance to combat the global burden of viral infections. Traditional antiviral drug development involves targeting specific viral proteins, which may lead to the emergence of resistant strains. To explore alternative strategies, we investigated the antiviral potential of antimicrobial peptidomimetic compounds. In this study, we evaluated the antiviral potential of 17 short anthranilamide-based peptidomimetic compounds against two viruses: Murine hepatitis virus 1 (MHV-1) which is a surrogate of human coronaviruses and herpes simplex virus 1 (HSV-1). The half-maximal inhibitory concentration (IC₅₀) values of these compounds were determined in vitro to assess their potency as antiviral agents. Compounds 11 and 14 displayed the most potent inhibitory effects with IC₅₀ values of 2.38 μM, and 6.3 μM against MHV-1 while compounds 9 and 14 showed IC₅₀ values of 14.8 μM and 13 μM against HSV-1. Multiple antiviral assessments and microscopic images obtained through transmission electron microscopy (TEM) collectively demonstrated that these compounds exert a direct influence on the viral envelope. Based on this outcome, it can be concluded that peptidomimetic compounds could offer a new approach for the development of potent antiviral agents. Full article

(This article belongs to the Special Issue Editorial Board Members' Collection Series: Structural Aspects of AMPs and Antimicrobials)

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13 pages, 2132 KiB

Open AccessArticle

Identification of an Antimicrobial Peptide from the Venom of the Trinidad Thick-Tailed Scorpion Tityus trinitatis with Potent Activity against ESKAPE Pathogens and Clostridioides difficile

by Milena Mechkarska, Taylor S. Cunning, Megan G. Taggart, Nigel G. Ternan, Jérôme Leprince, Laurent Coquet, Thierry Jouenne, Jordi Tena-Garcés, Juan J. Calvete and J. Michael Conlon

Antibiotics 2023, 12(9), 1404; https://0-doi-org.brum.beds.ac.uk/10.3390/antibiotics12091404 - 04 Sep 2023

Cited by 2 | Viewed by 1242

Abstract

Envenomation by the Trinidad thick-tailed scorpion Tityus trinitatis may result in fatal myocarditis and there is a high incidence of acute pancreatitis among survivors. Peptidomic analysis (reversed-phase HPLC followed by MALDI-TOF mass spectrometry and automated Edman degradation) of T. trinitatis venom led to the isolation and characterization of three peptides with antimicrobial activity. Their primary structures were established asTtAP-1 (FLGSLFSIGSKLLPGVFKLFSRKKQ.NH2), TtAP-2 (IFGMIPGLIGGLISAFK.NH2) and TtAP-3 (FFSLIPSLIGGLVSAIK.NH2). In addition, potassium channel and sodium channel toxins, present in the venom in high abundance, were identified by CID-MS/MS sequence analysis. TtAP-1 was the most potent against a range of clinically relevant Gram-positive and Gram-negative aerobes and against the anaerobe Clostridioides difficile (MIC = 3.1–12.5 µg/mL). At a concentration of 1× MIC, TtAP-1 produced rapid cell death (<15 min against Acinetobacter baumannii and Staphylococcus aureus). The therapeutic potential of TtAP-1 as an anti-infective agent is limited by its high hemolytic activity (LC₅₀ = 18 µg/mL against mouse erythrocytes) but the peptide constitutes a template for the design of analogs that maintain the high bactericidal activity against ESKAPE pathogens but are less toxic to human cells. It is suggested that the antimicrobial peptides in the scorpion venom facilitate the action of the neurotoxins by increasing the membrane permeability of cells from either prey or predator. Full article

(This article belongs to the Special Issue Editorial Board Members' Collection Series: Structural Aspects of AMPs and Antimicrobials)

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14 pages, 2397 KiB

Open AccessArticle

Purification, Conformational Analysis and Cytotoxic Activities of Host-Defense Peptides from the Giant Gladiator Treefrog Boana boans (Hylidae: Hylinae)

by J. Michael Conlon, Laure Guilhaudis, Samir Attoub, Laurent Coquet, Jérôme Leprince, Thierry Jouenne and Milena Mechkarska

Antibiotics 2023, 12(7), 1102; https://0-doi-org.brum.beds.ac.uk/10.3390/antibiotics12071102 - 25 Jun 2023

Cited by 1 | Viewed by 1299

Abstract

Frogs from the extensive amphibian family Hylidae are a rich source of peptides with therapeutic potential. Peptidomic analysis of norepinephrine-stimulated skin secretions from the Giant Gladiator Treefrog Boana boans (Hylidae: Hylinae) collected in Trinidad led to the isolation and structural characterization of five host-defense peptides with limited structural similarity to figainin 2 and picturin peptides from other frog species belonging to the genus Boana. In addition, the skin secretions contained high concentrations of tryptophyllin-BN (WRPFPFL) in both C-terminally α-amidated and non-amidated forms. Figainin 2BN (FLGVALKLGKVLG KALLPLASSLLHSQ) and picturin 1BN (GIFKDTLKKVVAAVLTTVADNIHPK) adopt α-helical conformations in trifluroethanol–water mixtures and in the presence of cell membrane models (sodium dodecylsulfate and dodecylphosphocholine micelles). The CD data also indicate contributions from turn structures. Both peptides and picturin 2BN (GLMDMLKKVGKVALT VAKSALLP) inhibited the growth of clinically relevant Gram-negative and Gram-positive bacteria with MIC values in the range 7.8–62.5 µM. Figainin 2BN was potently cytotoxic to A549, MDA-MB-231 and HT-29 human tumor-derived cells (LC₅₀ = 7–14 µM) but displayed comparable potency against non-neoplastic HUVEC cells (LC₅₀ = 15 µM) indicative of lack of selectivity for cancer cells. Full article

(This article belongs to the Special Issue Editorial Board Members' Collection Series: Structural Aspects of AMPs and Antimicrobials)

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Review

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20 pages, 1176 KiB

Open AccessReview

Diversity and Mechanisms of Action of Plant, Animal, and Human Antimicrobial Peptides

by Galina Satchanska, Slavena Davidova and Alexandra Gergova

Antibiotics 2024, 13(3), 202; https://0-doi-org.brum.beds.ac.uk/10.3390/antibiotics13030202 - 21 Feb 2024

Viewed by 1316

Abstract

Antimicrobial peptides (AMPs) are usually made up of fewer than 100 amino acid residues. They are found in many living organisms and are an important factor in those organisms’ innate immune systems. AMPs can be extracted from various living sources, including bacteria, plants, animals, and even humans. They are usually cationic peptides with an amphiphilic structure, which allows them to easily bind and interact with the cellular membranes of viruses, bacteria, fungi, and other pathogens. They can act against both Gram-negative and Gram-positive pathogens and have various modes of action against them. Some attack the pathogens’ membranes, while others target their intracellular organelles, as well as their nucleic acids, proteins, and metabolic pathways. A crucial area of AMP use is related to their ability to help with emerging antibiotic resistance: some AMPs are active against resistant strains and are susceptible to peptide engineering. This review considers AMPs from three key sources—plants, animals, and humans—as well as their modes of action and some AMP sequences. Full article

(This article belongs to the Special Issue Editorial Board Members' Collection Series: Structural Aspects of AMPs and Antimicrobials)

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14 pages, 1518 KiB

Open AccessReview

Peptide Stapling Applied to Antimicrobial Peptides

by Ana Laura Pereira Lourenço, Thuanny Borba Rios, Állan Pires da Silva, Octávio Luiz Franco and Marcelo Henrique Soller Ramada

Antibiotics 2023, 12(9), 1400; https://0-doi-org.brum.beds.ac.uk/10.3390/antibiotics12091400 - 02 Sep 2023

Cited by 2 | Viewed by 1313

Abstract

Antimicrobial peptides (AMPs) are considered a promising therapeutic approach against multi-drug resistant microorganisms. Besides their advantages, there are limitations to be overcome so that these molecules can become market competitive. One of the biggest limitations is proteolytic susceptibility, which could be overcome by structural modifications such as cyclization, especially for helix-constraining strategies. Over the years, many helix stabilization techniques have arisen, such as lactam-bridging, triazole-based, N-alkylation and all-hydrocarbon stapling. All-hydrocarbon stapling takes advantage of modified amino acid residues and olefinic cross-linking to constrain peptide helices. Despite being a well-established strategy and presenting efficient stability results, there are different limitations especially related to toxicity. In this review, recent studies on stapled AMPs for antimicrobial usage are explored with the aim of understanding the future of these molecules as putative antimicrobial agents. Full article

(This article belongs to the Special Issue Editorial Board Members' Collection Series: Structural Aspects of AMPs and Antimicrobials)

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Other

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14 pages, 2061 KiB

Open AccessPerspective

Dynamics-Based Regulatory Switches of Type II Antitoxins: Insights into New Antimicrobial Discovery

by Ki-Young Lee and Bong-Jin Lee

Antibiotics 2023, 12(4), 637; https://0-doi-org.brum.beds.ac.uk/10.3390/antibiotics12040637 - 23 Mar 2023

Cited by 1 | Viewed by 1637

Abstract

Type II toxin-antitoxin (TA) modules are prevalent in prokaryotes and are involved in cell maintenance and survival under harsh environmental conditions, including nutrient deficiency, antibiotic treatment, and human immune responses. Typically, the type II TA system consists of two protein components: a toxin that inhibits an essential cellular process and an antitoxin that neutralizes its toxicity. Antitoxins of type II TA modules typically contain the structured DNA-binding domain responsible for TA transcription repression and an intrinsically disordered region (IDR) at the C-terminus that directly binds to and neutralizes the toxin. Recently accumulated data have suggested that the antitoxin’s IDRs exhibit variable degrees of preexisting helical conformations that stabilize upon binding to the corresponding toxin or operator DNA and function as a central hub in regulatory protein interaction networks of the type II TA system. However, the biological and pathogenic functions of the antitoxin’s IDRs have not been well discussed compared with those of IDRs from the eukaryotic proteome. Here, we focus on the current state of knowledge about the versatile roles of IDRs of type II antitoxins in TA regulation and provide insights into the discovery of new antibiotic candidates that induce toxin activation/reactivation and cell death by modulating the regulatory dynamics or allostery of the antitoxin. Full article

(This article belongs to the Special Issue Editorial Board Members' Collection Series: Structural Aspects of AMPs and Antimicrobials)

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