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Antimicrobial Peptides: Biosynthesis, Molecular Mechanisms and Biomedical Applications

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

Deadline for manuscript submissions: 30 October 2026 | Viewed by 119

Editors


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Guest Editor
Instituto de Química Biológica, Universidad Nacional de Tucuman (UNT), San Miguel de Tucuman, Argentina
Interests: antimicrobial peptides; phenolic compounds

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Guest Editor Assistant
Instituto de Química Biológica, Universidad Nacional de Tucuman (UNT), San Miguel de Tucuman, Argentina
Interests: antimicrobial peptides

Special Issue Information

Dear Colleagues,

The rapid rise of antimicrobial resistance has intensified the search for alternatives to conventional antibiotics. Antimicrobial peptides (AMPs), including bacteriocins and other ribosomally and non-ribosomally synthesized peptides, have emerged as promising candidates due to their diverse mechanisms of action, broad-spectrum activity, and potential for engineering and optimization.

We are pleased to invite you to contribute to this Special Issue. It aims to highlight recent advances in the discovery, molecular characterization, and application of AMPs, in line with the journal’s focus on innovative antimicrobial strategies and mechanistic insights into bioactive compounds.

Original research articles and reviews are welcome. Research areas may include (but are not limited to): AMP biosynthesis and regulation, heterologous expression systems, mechanisms of action, AI-driven peptide design, peptide engineering and stability, pharmacokinetics and pharmacodynamics, nanoformulations, and emerging applications, including anticancer and immunomodulatory activities.

We look forward to receiving your contributions.

Dr. Carlos Minahk
Guest Editor

Dr. Lucía Lanza
Guest Editor Assistant

Manuscript Submission Information

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Keywords

  • antimicrobial peptides (AMPs)
  • bacteriocins
  • antimicrobial resistance
  • ribosomally synthesized peptides
  • non-ribosomal peptides
  • mechanism of action
  • structure–function relationship
  • artificial intelligence in peptide design
  • peptide engineering
  • pharmacokinetics and pharmacodynamics

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Published Papers (1 paper)

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Research

16 pages, 3351 KB  
Article
Decoding the Microcin J25 Biosynthetic Cluster: Modulation of the mcjA Promoter by the Novel Overlapping Gene mcjX
by Emilse Masias, Juan I. Ramirez, Lucía Lanza, Jorge A. Lachenicht, María E. Vázquez, Leonardo Acuña, Carlos J. Minahk and Raul A. Salomón
Int. J. Mol. Sci. 2026, 27(13), 5741; https://doi.org/10.3390/ijms27135741 - 25 Jun 2026
Abstract
A comprehensive analysis of the microcin J25 (MccJ25) biosynthetic gene cluster revealed a previously uncharacterized 96-base pair overlapping gene, designated mcjX. This gene features a +1 reading frame shift relative to the primary sequence and encodes a 31-amino acid peptide. Notably, 53 [...] Read more.
A comprehensive analysis of the microcin J25 (MccJ25) biosynthetic gene cluster revealed a previously uncharacterized 96-base pair overlapping gene, designated mcjX. This gene features a +1 reading frame shift relative to the primary sequence and encodes a 31-amino acid peptide. Notably, 53 nucleotides overlap with the 3′ terminus of the structural gene mcjA. Such significant overlaps are rare features in the Escherichia coli genome, highlighting the hidden complexity of microbial operon architectures. In this study, we demonstrate that mcjX is actively translated. Functional assays, including green fluorescent protein reporter systems, suggest that McjX acts as a negative regulator of the mcjA promoter, modulating MccJ25 expression. This discovery represents the first report of a regulatory mechanism mediated by an overlapping gene within a lasso peptide operon, providing new perspectives on how microbial genomes fine-tune the production of antimicrobial peptides through compact genetic organization. Full article
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