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Antimicrobial Peptide Assemblies

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Chemical Biology".

Deadline for manuscript submissions: 31 August 2026 | Viewed by 1884

Special Issue Editor


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Guest Editor
College of Chemistry, Jilin University, Changchun, China
Interests: peptide assembly; polycondensate; underwater adhesive; antimicrobial; tissue sealant
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Special Issue Information

Dear Colleagues,

Antimicrobial peptides have emerged as a promising therapeutic alternative for combating bacterial infections. Extensive research has documented their dual advantages in addressing infectious diseases while countering antimicrobial resistance. Recent advances in peptide assembly mark a significant milestone in enhancing pharmaceutical performance—particularly in optimizing antimicrobial efficacy, improving proteolytic resistance, and achieving the cost-effective production of short peptide sequences. Furthermore, self-assembled peptide nanostructures demonstrate unique capabilities in prolonging systemic circulation time, enhancing cellular internalization efficiency, and facilitating targeted delivery with preferential bacterial membrane accumulation. Crucially, the inherent dynamic assembly and disassembly feature endows these nanomaterials with stimuli-responsive behavior, creating novel opportunities for developing intelligent antimicrobial systems capable of on-demand drug release at infection sites.

This Special Issue seeks to compile cutting-edge research and comprehensive reviews focusing on four key dimensions of self-assembling antimicrobial peptide systems: (1) rational design principles guiding nanostructure formation; (2) innovative fabrication methodologies for functional assemblies; (3) mechanistic studies elucidating structure-activity correlations; and (4) optimization strategies balancing antimicrobial potency with biosafety profiles. We particularly welcome contributions that advance fundamental understanding of peptide assembly–disassembly dynamics, develop characterization platforms for nanostructure–bacteria interactions, and establish sound design rules for self-assembling antimicrobial peptides.

Prof. Dr. Wen Li
Guest Editor

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Keywords

  • peptides
  • peptide hybrids
  • peptide conjugates
  • self-assembly
  • stimuli-responsiveness
  • antimicrobial activity

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Published Papers (2 papers)

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Review

35 pages, 1717 KB  
Review
The Potential of Non-Ribosomal Peptide Engineering for Creating New Antimicrobial Complexes
by Evgeniya V. Prazdnova, Maxim P. Kulikov and Ludmila E. Khmelevtsova
Molecules 2026, 31(4), 683; https://doi.org/10.3390/molecules31040683 - 16 Feb 2026
Viewed by 634
Abstract
Self-assembling antimicrobial complexes are a promising new technology for the development of antimicrobial, antifungal, and other bioactive agents with targeted delivery, adaptability, and the regulation of processes over time. Ribosomally synthesized antimicrobial peptides (AMPs) are most frequently considered as the basis for such [...] Read more.
Self-assembling antimicrobial complexes are a promising new technology for the development of antimicrobial, antifungal, and other bioactive agents with targeted delivery, adaptability, and the regulation of processes over time. Ribosomally synthesized antimicrobial peptides (AMPs) are most frequently considered as the basis for such complexes; however, we suggest that non-ribosomally synthesized peptides (NRPs) should be considered as molecules that also hold potential for engineering and already possess a set of qualities that AMPs are still to be engineered to have. This review examines the key features of NRP structure and self-assembly that determine their potential as antimicrobial agents, as well as NRP engineering methods through which new, more advanced agents for combating antibiotic-resistant microorganisms can be created. Full article
(This article belongs to the Special Issue Antimicrobial Peptide Assemblies)
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28 pages, 84682 KB  
Review
Antimicrobial Peptide Nanoassemblies: Design, Response Mechanisms, and Biomedical Applications
by Tao Wang, Linbao Ji, Yucheng Zhang, Zhili Niu, Xiaoyi Jiang, Xingyao Wang, Qingtai Zhang, Yuting Zhang, Peng Tan, Yue Feng, Xi Ma and Zhihong Sun
Molecules 2026, 31(3), 518; https://doi.org/10.3390/molecules31030518 - 2 Feb 2026
Viewed by 911
Abstract
The overuse of antibiotics has accelerated the evolution and mutation of drug-resistant bacteria, creating an urgent need for novel antimicrobial drugs and feed additives. Antimicrobial peptides, with their unique membrane-disrupting mechanism that resists the development of resistance, hold promise as antibiotic alternatives. To [...] Read more.
The overuse of antibiotics has accelerated the evolution and mutation of drug-resistant bacteria, creating an urgent need for novel antimicrobial drugs and feed additives. Antimicrobial peptides, with their unique membrane-disrupting mechanism that resists the development of resistance, hold promise as antibiotic alternatives. To overcome the limitations of natural antimicrobial peptides—such as poor stability, susceptibility to protease degradation, and short in vivo half-lives—self-assembling peptide technology has emerged. This approach employs non-covalent interactions to orderly assemble monomeric peptides into stable, structured nanomaterials like nanofibers, nanotubes, and hydrogels. This paper outlines the molecular design principles and smart response mechanisms of antimicrobial peptide nanoassemblies, elucidates their core advantages over monomeric peptides, summarizes their application scenarios in anti-infection fields, and discusses limitations and future directions across various domains. It provides insights for future antimicrobial peptide design. Full article
(This article belongs to the Special Issue Antimicrobial Peptide Assemblies)
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