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Antibiotics
Special Issues
Antimicrobial Peptides: Mechanisms, Engineering, and Therapeutic Development
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Antimicrobial Peptides: Mechanisms, Engineering, and Therapeutic Development

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

Deadline for manuscript submissions: 31 December 2026 | Viewed by 3587

Special Issue Editors

Prof. Dr. Feng-Di Lung

E-Mail Website
Guest Editor
Department of Chemistry, Tonghai University, Taichung, Taiwan
Interests: development of functional peptides, such as antimicrobial peptides and anti-cancer peptides
Special Issues, Collections and Topics in MDPI journals
Dr. Kuang-Li Peng

E-Mail Website
Co-Guest Editor
Department of Medical Science, Institute of Biotechnology, National Tsing Hua University, Hsinchu 300, Taiwan
Interests: antimicrobial peptide; drug design; structural biology

Special Issue Information

Dear Colleagues,

The emergence of multidrug-resistant pathogens poses a major global health threat and underscores the urgent need for novel therapeutic strategies. Antimicrobial peptides (AMPs) have attracted significant attention as promising alternatives or adjuncts to conventional antibiotics due to their broad-spectrum activity, rapid killing mechanisms, and immunomodulatory functions. Recent advances in peptide design, synthetic biology, and delivery technologies have expanded the therapeutic potential of AMPs, moving them closer to clinical application. This Special Issue of Antibiotics will highlight recent progress in the discovery, molecular mechanisms, structural engineering, and therapeutic development of antimicrobial peptides. We aim to bring together original research articles, reviews, and perspectives that provide new insights into the role of AMPs in combating infections and addressing antimicrobial resistance. By gathering cutting-edge research and comprehensive reviews, this Special Issue aims to foster interdisciplinary collaboration and accelerate the translation of antimicrobial peptides into effective clinical solutions.

Prof. Dr. Feng-Di Lung
Guest Editor

Dr. Kuang-Li Peng
Co-Guest Editor

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 250 words) can be sent to the Editorial Office for assessment.

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

  • antimicrobial peptides (AMPs)
  • peptide engineering
  • mechanisms of action
  • antibiotic resistance
  • host defense peptides
  • immunomodulation
  • drug delivery systems
  • synergy with antibiotics
  • therapeutic development
  • computational peptide design

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Published Papers (2 papers)

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Research

19 pages, 6536 KB  
Article
Development of New Antimicrobial Peptides by Directional Selection
by Ekaterina Grafskaia, Pavel Bobrovsky, Daria Kharlampieva, Ksenia Brovina, Maria Serebrennikova, Sabina Alieva, Oksana Selezneva, Ekaterina Bessonova, Vassili Lazarev and Valentin Manuvera
Antibiotics 2025, 14(11), 1120; https://doi.org/10.3390/antibiotics14111120 - 6 Nov 2025
Viewed by 1922
Abstract
Background/Objectives: The global rise in antibiotic resistance necessitates the development of novel antimicrobial agents. Antimicrobial peptides (AMPs), key components of innate immunity, are promising candidates. This study aimed to develop novel therapeutic peptides with enhanced properties through the mutagenesis of natural AMPs [...] Read more.
Background/Objectives: The global rise in antibiotic resistance necessitates the development of novel antimicrobial agents. Antimicrobial peptides (AMPs), key components of innate immunity, are promising candidates. This study aimed to develop novel therapeutic peptides with enhanced properties through the mutagenesis of natural AMPs and high-throughput screening. Methods: We constructed mutant libraries of three broad-spectrum AMPs—melittin, cecropin, and Hm-AMP2—using mutagenesis with partially degenerate oligonucleotides. Libraries were expressed in Escherichia coli, and antimicrobial activity was assessed through bacterial growth kinetics and droplet serial dilution assays. Candidate molecules were identified by DNA sequencing, and the most promising variants were chemically synthesized. Antimicrobial activity was determined by minimal inhibitory concentration (MIC) against E. coli and Bacillus subtilis, while cytotoxicity was evaluated in human Expi293F cells (IC90) viability. The therapeutic index was calculated as the ratio of an AMP’s cytotoxic concentration to its effective antimicrobial concentration. Results: Mutant forms of melittin (MR1P7, MR1P8) showed significantly reduced cytotoxicity while retaining antimicrobial activity. Cecropin mutants exhibited reduced efficacy against E. coli, but variants CR2P2, CR2P7, and CR2P8 gained activity against Gram-positive bacteria. Mutagenesis of Hm-AMP2 generally decreased activity against E. coli, though two variants (A2R1P5 and A2R3P6) showed retained or enhanced efficacy against B. subtilis while maintaining low cytotoxicity. Conclusions: The proposed strategy successfully generated peptides with improved therapeutic profiles, including reduced toxicity or a broader spectrum of antimicrobial activity, despite not improving all parameters. This approach enables the discovery of novel bioactive peptides to combat antibiotic-resistant pathogens. Full article
(This article belongs to the Special Issue Antimicrobial Peptides: Mechanisms, Engineering, and Therapeutic Development)
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21 pages, 1579 KB  
Article
Sequence Permutation Generated Lysine and Tryptophan-Rich Antimicrobial Peptides with Enhanced Therapeutic Index
by Kuang-Li Peng, Yu-Hsuan Wu, Hsuan-Che Hsu and Jya-Wei Cheng
Antibiotics 2025, 14(11), 1077; https://doi.org/10.3390/antibiotics14111077 - 26 Oct 2025
Cited by 1 | Viewed by 1369
Abstract
Background/Objectives: Antimicrobial peptides (AMPs) are promising therapeutic agents due to their broad-spectrum activity against bacteria, viruses, and fungi. Unlike traditional antibiotics, AMPs target microbial membranes directly and are less likely to induce resistance. They also possess immunomodulatory and wound-healing properties. However, clinical application [...] Read more.
Background/Objectives: Antimicrobial peptides (AMPs) are promising therapeutic agents due to their broad-spectrum activity against bacteria, viruses, and fungi. Unlike traditional antibiotics, AMPs target microbial membranes directly and are less likely to induce resistance. They also possess immunomodulatory and wound-healing properties. However, clinical application remains limited by factors such as salt sensitivity, low bioavailability, and poor stability. To address these challenges, researchers have turned to structural optimization strategies. Recently, artificial intelligence (AI) has facilitated peptide drug design by rapidly screening large peptide libraries. Still, AI struggles to predict how subtle sequence changes affect peptide structure and function. Traditional sequence permutation offers a complementary approach by analyzing structural and functional effects without altering amino acid composition. Methods: In this study, we applied a clockwise sequence permutation strategy to the AMP W5K/A9W, generating derivative peptides with identical molecular weight, net charge, and hydrophobicity. We aimed to investigate how lysine and tryptophan distribution affects antimicrobial activity, membrane permeability, and selectivity. We assessed the secondary structures using circular dichroism (CD) spectroscopy and evaluated in vitro antimicrobial activity, salt resistance, membrane-permeabilizing ability, hemolysis, and wound healing effects. Results: The results revealed that the sequence arrangement of key residues significantly impacts peptide bioactivity and therapeutic index. Conclusions: This study highlights the importance of sequence order in determining AMP function. It also supports integrating permutation strategies with AI-based design to enhance AMP discovery. Together, these approaches offer new opportunities to combat drug-resistant pathogens and advance next-generation anti-infective therapies. Full article
(This article belongs to the Special Issue Antimicrobial Peptides: Mechanisms, Engineering, and Therapeutic Development)
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