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Antibiotics
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Insights into Natural Antimicrobial Peptides
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Insights into Natural Antimicrobial Peptides

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

Deadline for manuscript submissions: 31 May 2025 | Viewed by 11728

Special Issue Editors

Dr. András Fodor

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Guest Editor
Department of Genetics, Eötvös Loránd University, Pázmány P. Sétány 1C, H-1117 Budapest, Hungary
Interests: nematode genetics; nematode/bacterium symbioses; antimicrobial peptides; plant immunity
Special Issues, Collections and Topics in MDPI journals
Dr. Eustachio Tarasco

E-Mail Website
Guest Editor
Department of Soil, Plant and Food Sciences, University of Bari “Aldo Moro”, via Amendola 165/A, 70126 Bari, Italy
Interests: microbial control; entomopathogenic nematodes and fungi biodiversity; forest and urban entomology
Special Issues, Collections and Topics in MDPI journals
Dr. Maurizio Francesco Brivio

E-Mail Website
Guest Editor
Laboratory of Comparative Immunology and Parasitology, University of Insubria, 21100 Varese, Italy
Interests: insect immunity; innate immunity; parasitology; nematodes; host–parasite interaction
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The speed of the spread of multidrug resistance (MDR) in both prokaryotic and eukaryotic pathogen organisms is an alarming message for scientists, necessitating a search for ways to block this dangerous trend. The discovery and chemotherapeutic application of novel antimicrobial peptide (AMP) drugs seem to offer a prospective alternative research direction. The arguments for AMPs application include slower emergence of resistance, broad-spectral antibiofilm activity, and the ability to interact synergistically with the host immune system. AMP-resistant bacteria tend to exhibit collateral sensitivity to antibiotics, and the mobility patterns of traditional AMP-resistance genes are different from those of the conventional antibiotics-resistance genes and do not induce drastic changes in the composition of the gut microbiota. These molecules are peptides, that is polyamides and their copolymers with esters, thioesters, or otherwise modified backbones. They can be found in nature, or prepared with a contemporary chemical peptide synthesizer. This provides an option for benefitting from the available toolkit of QASR-based design for obtaining more efficient analogs with fewer side effects. As for the publication criteria: original research papers and reviews, - focusing either on theoretical, or application aspects, - reports on discoveries, chemical and biological novelties, application perspectives, bioassays, and synergetic studies are warmly welcome.

Dr. András Fodor
Dr. Eustachio Tarasco
Dr. Maurizio Francesco Brivio
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.

Keywords

  • antibacterial host defense peptides
  • antibacterial mode of action
  • defensins
  • cathelicidins
  • insect antimicrobial peptides
  • plant antimicrobial peptides

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Published Papers (4 papers)

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Research

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22 pages, 7870 KiB  
Article
In Vitro/Vivo Mechanisms of Antibacterial Peptide NZ2114 against Staphylococcus pseudintermedius and Its Biofilms
by Shuang Zhang, Na Yang, Ruoyu Mao, Ya Hao, Da Teng and Jianhua Wang
Antibiotics 2024, 13(4), 341; https://doi.org/10.3390/antibiotics13040341 - 8 Apr 2024
Cited by 3 | Viewed by 2296
Abstract
Staphylococcus pseudintermedius is an opportunistic pathogen commonly found in canines, and has garnered escalating interest due to its potential for zoonotic transmission and increasing antimicrobial resistance. However, the excessive use of antibiotics and the characteristic of S. pseudintermedius forming biofilms make treatment challenging. [...] Read more.
Staphylococcus pseudintermedius is an opportunistic pathogen commonly found in canines, and has garnered escalating interest due to its potential for zoonotic transmission and increasing antimicrobial resistance. However, the excessive use of antibiotics and the characteristic of S. pseudintermedius forming biofilms make treatment challenging. In this study, the in vivo and in vitro antimicrobial activity and mechanisms of action of NZ2114, a plectasin-derived peptide, against S. pseudintermedius were investigated. NZ2114 exhibited potent antibacterial activity towards S. pseudintermedius (minimum inhibitory concentration, MIC = 0.23 μM) with a lower probability of inducing drug-resistant mutations and efficient bactericidal action, which was superior to those of mopirucin (MIC = 0.25–0.5 μM) and lincomycin (MIC = 4.34–69.41 μM). The results of electron microscopy and flow cytometry showed that NZ2114 disrupted S. pseudintermedius’ cell membrane, resulting in cellular content leakage, cytoplasmic membrane shrinkage, and, eventually, cell death. The intracellular ROS activity and Alamar Blue detection showed that NZ2114 interferes with intracellular metabolic processes. In addition, NZ2114 effectively inhibits biofilm formation, and confocal laser scanning microscopy further revealed its antibacterial and anti-biofilm activity (biofilm thickness reduced to 6.90–17.70 μm). The in vivo therapy of NZ2114 in a mouse pyoderma model showed that it was better than lincomycin in effectively decreasing the number of skin bacteria, alleviating histological damage, and reducing the skin damage area. These results demonstrated that NZ2114 may be a promising antibacterial candidate against S. pseudintermedius infections. Full article
(This article belongs to the Special Issue Insights into Natural Antimicrobial Peptides)
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13 pages, 3934 KiB  
Article
Anti-Salmonella Activity of a Novel Peptide, KGGDLGLFEPTL, Derived from Egg Yolk Hydrolysate
by Thippawan Pimchan, Fu Tian, Kanjana Thumanu, Sureelak Rodtong and Jirawat Yongsawatdigul
Antibiotics 2024, 13(1), 19; https://doi.org/10.3390/antibiotics13010019 - 24 Dec 2023
Cited by 2 | Viewed by 2487
Abstract
The present study aimed to characterize the mode of action of a novel antimicrobial peptide isolated from egg yolk hydrolysate. The EYHp6, KGGDLGLFEPTL, exhibited inhibition against Salmonella enterica serovar Typhimurium TISTR 292 and S. enterica serovar Enteritidis DMST 15679 with a MIC value [...] Read more.
The present study aimed to characterize the mode of action of a novel antimicrobial peptide isolated from egg yolk hydrolysate. The EYHp6, KGGDLGLFEPTL, exhibited inhibition against Salmonella enterica serovar Typhimurium TISTR 292 and S. enterica serovar Enteritidis DMST 15679 with a MIC value of 2 mM. In contrast, S. enterica serovar Newport ATCC 6962 and other strains of Typhimurium and Enteritidis were inhibited at 4 mM. EYHp6 increased the cell membrane permeability of S. Typhimurium TISTR 292, leading to DNA leakage. Membrane integrity determined by propidium iodide and SYTO9 staining visualized by confocal microscopy demonstrated that EYHp6 at 1 × MIC induced disruption of cell membranes. Electron microscopy revealed that treatment of S. Typhimurium with EYHp6 led to damage to the cell membrane, causing the leakage of intracellular contents. Synchrotron-based Fourier-transform infrared spectroscopy indicated that EYHp6 killed S. Typhimurium by targeting fatty acids and nucleic acids in the cell membrane. The peptide did not show hemolytic activity up to 4 mM. These findings suggest that EYHp6 could be a promising antibacterial agent for controlling the growth of S. enterica. Full article
(This article belongs to the Special Issue Insights into Natural Antimicrobial Peptides)
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Review

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31 pages, 2559 KiB  
Review
Origami of KR-12 Designed Antimicrobial Peptides and Their Potential Applications
by Jayaram Lakshmaiah Narayana, Abraham Fikru Mechesso, Imran Ibni Gani Rather, D. Zarena, Jinghui Luo, Jingwei Xie and Guangshun Wang
Antibiotics 2024, 13(9), 816; https://doi.org/10.3390/antibiotics13090816 - 28 Aug 2024
Cited by 4 | Viewed by 3091
Abstract
This review describes the discovery, structure, activity, engineered constructs, and applications of KR-12, the smallest antibacterial peptide of human cathelicidin LL-37, the production of which can be induced under sunlight or by vitamin D. It is a moonlighting peptide that shows both antimicrobial [...] Read more.
This review describes the discovery, structure, activity, engineered constructs, and applications of KR-12, the smallest antibacterial peptide of human cathelicidin LL-37, the production of which can be induced under sunlight or by vitamin D. It is a moonlighting peptide that shows both antimicrobial and immune-regulatory effects. Compared to LL-37, KR-12 is extremely appealing due to its small size, lack of toxicity, and narrow-spectrum antimicrobial activity. Consequently, various KR-12 peptides have been engineered to tune peptide activity and stability via amino acid substitution, end capping, hybridization, conjugation, sidechain stapling, and backbone macrocyclization. We also mention recently discovered peptides KR-8 and RIK-10 that are shorter than KR-12. Nano-formulation provides an avenue to targeted delivery, controlled release, and increased bioavailability. In addition, KR-12 has been covalently immobilized on biomaterials/medical implants to prevent biofilm formation. These constructs with enhanced potency and stability are demonstrated to eradicate drug-resistant pathogens, disrupt preformed biofilms, neutralize endotoxins, and regulate host immune responses. Also highlighted are the safety and efficacy of these peptides in various topical and systemic animal models. Finaly, we summarize the achievements and discuss future developments of KR-12 peptides as cosmetic preservatives, novel antibiotics, anti-inflammatory peptides, and microbiota-restoring agents. Full article
(This article belongs to the Special Issue Insights into Natural Antimicrobial Peptides)
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19 pages, 6738 KiB  
Review
Short-Chained Linear Scorpion Peptides: A Pool for Novel Antimicrobials
by Tolis Panayi, Spiridoula Diavoli, Vicky Nicolaidou, Christos Papaneophytou, Christos Petrou and Yiannis Sarigiannis
Antibiotics 2024, 13(5), 422; https://doi.org/10.3390/antibiotics13050422 - 5 May 2024
Cited by 3 | Viewed by 2917
Abstract
Scorpion venom peptides are generally classified into two main groups: the disulfide bridged peptides (DBPs), which usually target membrane-associated ion channels, and the non-disulfide bridged peptides (NDBPs), a smaller group with multifunctional properties. In the past decade, these peptides have gained interest because [...] Read more.
Scorpion venom peptides are generally classified into two main groups: the disulfide bridged peptides (DBPs), which usually target membrane-associated ion channels, and the non-disulfide bridged peptides (NDBPs), a smaller group with multifunctional properties. In the past decade, these peptides have gained interest because most of them display functions that include antimicrobial, anticancer, haemolytic, and anti-inflammatory activities. Our current study focuses on the short (9–19 amino acids) antimicrobial linear scorpion peptides. Most of these peptides display a net positive charge of 1 or 2, an isoelectric point at pH 9–10, a broad range of hydrophobicity, and a Grand Average of Hydropathy (GRAVY) Value ranging between −0.05 and 1.7. These features allow these peptides to be attracted toward the negatively charged phospholipid head groups of the lipid membranes of target cells, a force driven by electrostatic interactions. This review outlines the antimicrobial potential of short-chained linear scorpion venom peptides. Additionally, short linear scorpion peptides are in general more attractive for large-scale synthesis from a manufacturing point of view. The structural and functional diversity of these peptides represents a good starting point for the development of new peptide-based therapeutics. Full article
(This article belongs to the Special Issue Insights into Natural Antimicrobial Peptides)
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