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Peptide Antimicrobial Agents 2.0
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Peptide Antimicrobial Agents 2.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biophysics".

Deadline for manuscript submissions: closed (15 December 2021) | Viewed by 5748

Special Issue Editors

Prof. Dr. Gábor Tóth

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Guest Editor
Department of Medical Chemistry, Faculty of Medicine, University of Szeged, H-6720 Szeged, Hungary
Interests: protein and peptide synthesis; protein bioconjugation; bioactive peptides; bioorganic chemistry; synthesis of multiple disulfide containing polypeptides; posttranslationally modified peptides; ion channel blockers
Special Issues, Collections and Topics in MDPI journals
Dr. Györgyi Váradi

E-Mail Website
Guest Editor
Department of Medical Chemistry, Faculty of Medicine, University of Szeged, H-6720 Szeged, Hungary
Interests: antimicrobial peptides; antifungal proteins; structure-activity relationships of antifungal proteins; peptide and protein synthesis; native chemical ligation; selective formation of disulfide bridges
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Antibiotic resistance—when germs (bacteria and fungi) develop the ability to defeat the antibiotics designed to kill them—is one of the greatest global health challenges of modern time. Currently, at least 700,000 people die each year due to drug-resistant diseases, including 230,000 people who die from multidrug-resistant tuberculosis. More and more common diseases, including respiratory tract infections, sexually transmitted infections and urinary tract infections, are untreatable. The ever-increasing episodes of antibiotic resistance in bacteria and other microorganisms pose a serious threat to human health. Antimicrobial peptides (AMPs) are ribosomally synthesized natural antibiotics produced by nearly all organisms, from bacteria to plants and animals. AMPs are the first line of innate defense present in most living organisms, from bacteria to humans, against invading pathogens. Certain AMPs show an exceptionally broad spectrum of activity against Gram-negative and Gram-positive bacteria and fungi as well as viruses and parasites. Therefore, AMPs or their derivatives may represent potentially new classes of antimicrobial drugs. In this context, antimicrobial peptides (AMPs) have emerged as promising alternatives owing to their unique structural and functional characteristics. They have various modes of action; this diversity in the activity of the AMPs lead to the very-slow or negligible development of resistance against them in contrast to conventional antibiotics, which generally have a fixed intracellular target. This has led to significant advances in the area of AMP research in the last few decades for potential drugs of the future.

Prof. Dr. Gábor Tóth
Dr. Györgyi Váradi
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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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 (3 papers)

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Research

15 pages, 1286 KiB  
Article
The Potential Antimicrobial Action of Human Mucin 7 15-Mer Peptide and Its Metal Complexes
by Anna Janicka-Kłos, Hanna Czapor-Irzabek and Tomasz Janek
Int. J. Mol. Sci. 2022, 23(1), 418; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23010418 - 30 Dec 2021
Cited by 3 | Viewed by 1714
Abstract
Mucin 7 (encoded byMUC7) is a human salivary protein that has a role in the natural immune system. Fragments of mucin 7 exhibit antimicrobial activity against bacteria and yeast. Although the antimicrobial properties of peptides have been known and studied for decades, the [...] Read more.
Mucin 7 (encoded byMUC7) is a human salivary protein that has a role in the natural immune system. Fragments of mucin 7 exhibit antimicrobial activity against bacteria and yeast. Although the antimicrobial properties of peptides have been known and studied for decades, the exact mechanism of action of antimicrobial peptides (AMPs) is still unclear. It is known that some AMPs require divalent metal ions to activate their activity. Herein, we investigated three 15-mer MUC7 peptides, one of which (mother peptide, sequence, L3) is a synthetic analog of a fragment naturally excised from MUC7 (with His3, His8, and His 14) and its two structural analogs, containing only two histidine residues, His3, His13 and His8, His13 (L2 and L1, respectively). Since there is a correlation between lipophilicity, the presence of metal ions (such as Cu(II) and Zn(II)) and antimicrobial activity of AMP, antimicrobial properties of the studied peptides, as well as their complexes with Cu(II) and Zn(II) ions, were tested for activity against Gram-positive (Enterococcus faecalis, Staphylococcus epidermidis) and Gram-negative (Escherichia coli, Pseudomonas aeruginosa) bacteria and fungi (Candida albicans). The results were correlated with their lipophilicity. Coordination and thermodynamic studies (potentiometry, UV-Vis, CD) revealed the formation of mainly mononuclear complexes in solution for all studied systems with different stability in the physiological pH range. Full article
(This article belongs to the Special Issue Peptide Antimicrobial Agents 2.0)
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17 pages, 4975 KiB  
Article
Structure and Formation Mechanism of Antimicrobial Peptides Temporin B- and L-Induced Tubular Membrane Protrusion
by Shan Zhang, Ming Ma, Zhuang Shao, Jincheng Zhang, Lei Fu, Xiangyuan Li, Weihai Fang and Lianghui Gao
Int. J. Mol. Sci. 2021, 22(20), 11015; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms222011015 - 13 Oct 2021
Cited by 7 | Viewed by 1897
Abstract
Temporins are a family of antimicrobial peptides (AMPs) isolated from frog skin, which are very short, weakly charged, and highly hydrophobic. They execute bactericidal activities in different ways from many other AMPs. This work investigated morphological changes of planar bilayer membranes composed of [...] Read more.
Temporins are a family of antimicrobial peptides (AMPs) isolated from frog skin, which are very short, weakly charged, and highly hydrophobic. They execute bactericidal activities in different ways from many other AMPs. This work investigated morphological changes of planar bilayer membranes composed of mixed zwitterionic and anionic phospholipids induced by temporin B and L (TB and TL) using all-atom and coarse-grained molecular dynamics simulations. We found that TB and TL fold to α-helices at the membrane surface and penetrate shallowly into the bilayer. These short AMPs have low propensity to induce membrane pore formation but possess high ability to extract lipids out. At relatively high peptide concentrations, the strong hydrophobicity of TB and TL promotes them to aggregate into clusters on the membrane surface. These aggregates attract a large amount of lipids out of the membrane to release compression induced by other dispersed peptides binding to the membrane. The extruded lipids mix evenly with the peptides in the cluster and form tubule-like protrusions. Certain water molecules follow the movement of lipids, which not only fill the cavities of the protrusion but also assist in maintaining the tubular structures. In contrast, the peptide-free leaflet remains intact. The present results unravel distinctive antimicrobial mechanisms of temporins disturbing membranes. Full article
(This article belongs to the Special Issue Peptide Antimicrobial Agents 2.0)
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13 pages, 1686 KiB  
Article
The Central PXXP Motif Is Crucial for PMAP-23 Translocation across the Lipid Bilayer
by Sung-Tae Yang, Song-Yub Shin and Sung-Heui Shin
Int. J. Mol. Sci. 2021, 22(18), 9752; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22189752 - 09 Sep 2021
Cited by 7 | Viewed by 1669
Abstract
PMAP-23, a cathelicidin-derived host defense peptide, does not cause severe membrane permeabilization, but exerts strong and broad-spectrum bactericidal activity. We have previously shown that it forms an amphipathic α-helical structure with a central hinge induced by the PXXP motif, which is implicated in [...] Read more.
PMAP-23, a cathelicidin-derived host defense peptide, does not cause severe membrane permeabilization, but exerts strong and broad-spectrum bactericidal activity. We have previously shown that it forms an amphipathic α-helical structure with a central hinge induced by the PXXP motif, which is implicated in the interaction of PMAP-23 with negatively charged bacterial membranes. Here, we studied the potential roles of the PXXP motif in PMAP-23 translocation across the lipid bilayer by replacing Pro residues with either α-helix former Ala (PMAP-PA) or α-helix breaker Gly (PMAP-PG). Although both PMAP-PA and PMAP-PG led to effective membrane depolarization and permeabilization, they showed less antimicrobial activity than wild-type PMAP-23. Interestingly, we observed that PMAP-23 crossed lipid bilayers much more efficiently than its Pro-substituted derivatives. The fact that the Gly-induced hinge was unable to replace the PXXP motif in PMAP-23 translocation suggests that the PXXP motif has unique structural properties other than the central hinge. Surface plasmon resonance sensorgrams showed that the running buffer almost entirely dissociated PMAP-23 from the membrane surface, while its Pro-substituted derivatives remained significantly bound to the membrane. In addition, kinetic analysis of the sensorgrams revealed that the central PXXP motif allows PMAP-23 to rapidly translocate at the interface between the hydrophilic and hydrophobic phases. Taken together, we propose that the structural and kinetic understanding of the PXXP motif in peptide translocation could greatly aid the development of novel antimicrobial peptides with intracellular targets by promoting peptide entry into bacterial cells. Full article
(This article belongs to the Special Issue Peptide Antimicrobial Agents 2.0)
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