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Pharmaceutics
Special Issues
Antimicrobial Peptides as Promising Therapeutic Agents
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Antimicrobial Peptides as Promising Therapeutic Agents

A special issue of Pharmaceutics (ISSN 1999-4923). This special issue belongs to the section "Drug Targeting and Design".

Deadline for manuscript submissions: 7 March 2027 | Viewed by 3080

Special Issue Editors

Dr. Axel Hollmann

E-Mail Website
Guest Editor
Laboratorio de Compuestos Bioactivos, Centro de Investigaciones en Biofísica Aplicada y Alimentos (CIBAAL), CONICET—Universidad Nacional de Santiago del Estero, RN 9, Km 1125, 4206 Santiago del Estero, Argentina
Interests: antimicrobial peptides; peptide—membrane interactions; natural antimicrobials; green silver nanoparticles; essential oils as antimicrobials
Special Issues, Collections and Topics in MDPI journals
Dr. Paulo C Maffía

E-Mail Website
Guest Editor
Laboratorio de Aplicaciones Biotecnológicas y Microbiología (LAByM), Universidad Nacional de Hurlingham, Buenos Aires, Argentina
Interests: antimicrobial peptides; anti-inflammatory peptides; natural antimicrobial molecules; cannabinoids as antimicrobial molecules; antimicrobial resistant bacteria

Special Issue Information

Dear Colleagues,

Antimicrobial peptides (AMPs) have garnered considerable attention as novel agents with unique mechanisms of action that can circumvent the limitations of traditional antibiotics.

AMPs are natural antibiotics and anti-virals found in several organisms, including mammals, arthropods, plants, and bacteria, and they play a key role in the innate immune system. Their broad-spectrum antimicrobial activity makes them promising candidates for therapeutic applications.

This Special Issue focuses on research studies in AMPs, including the discovery and characterization of natural or designed AMPs, chemical modifications, formulation strategies, mechanisms of action, and innovative delivery systems. In addition, we welcome the submission of studies on synergistic activity with other molecules that aim to enhance the therapeutic potential of AMPs in the fight against resistant bacteria and viruses, as well as mechanisms of resistance against AMPs.

Dr. Axel Hollmann
Dr. Paulo C Maffía
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 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. Pharmaceutics 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
  • peptide–membrane interactions
  • antiviral peptides
  • mechanism of action
  • synergy
  • multi-drug-resistant bacteria
  • immune modulation

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Published Papers (3 papers)

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Research

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13 pages, 1576 KB  
Article
Leishmanicidal Action of the Peptides 19-4LF, 19-2.5 and 19-2.5LF Topically Administered on Cutaneous Lesions Caused by Leishmania major
by Rima El-Dirany, Paolo Ginatta, Celia Fernández-Rubio, Aroia Burguete-Mikeo, Esther Larrea, Guillermo Martinez-de-Tejada and Paul A. Nguewa
Pharmaceutics 2026, 18(3), 332; https://doi.org/10.3390/pharmaceutics18030332 - 7 Mar 2026
Viewed by 649
Abstract
Background/Objectives: Antimicrobial peptides (AMPs) represent a promising class of therapeutics with diverse biological functions, including antibacterial, anti-fungal, anti-parasitic and anti-tumoral activities. Previous works demonstrated the successful repurposing of the two synthetic AMPs 19-2.5 and 19-4LF for cutaneous leishmaniasis, when the compounds were administered [...] Read more.
Background/Objectives: Antimicrobial peptides (AMPs) represent a promising class of therapeutics with diverse biological functions, including antibacterial, anti-fungal, anti-parasitic and anti-tumoral activities. Previous works demonstrated the successful repurposing of the two synthetic AMPs 19-2.5 and 19-4LF for cutaneous leishmaniasis, when the compounds were administered in solution on skin lesions caused by Leishmania major in a BALB/c mouse model. In this research project, we assessed the activity of 19-4LF, 19-2.5, and their hybrid 19-2.5LF derivative when formulated as a cream for topical administration in the same animal model. Methods: The peptides were formulated in DAC cream and applied to the wound of BALB/C mice for 30 days. Lesion progression was monitored using a digital caliper. Parasite burden was measured by qPCR. Parasite viability was assessed using MTT and microscopy imaging assays. Results: The three peptides in cream formulation succeeded in reducing the skin lesion. Peptide 19-4LF was the most potent, followed by 19-2.5LF and then 19-2.5. In addition, 19-4LF was able to significantly reduce the parasite burden in the skin lesions of infected mice, as measured by quantifying L. major Lm18S ribosomal gene mRNA levels using qPCR. Moreover, when combined, the peptides exhibited synergistic effects on L. major promastigotes and significantly reduced the number of amastigotes in infected macrophages. Conclusions: These studies support the approach of repurposing these AMPs as antileishmanial drugs and identify 19-4LF as a lead candidate for further studies. While historical barriers to peptide therapeutics included high production costs, recent advancements in biological fermentation and synthesis strategies have significantly improved their economic viability. Furthermore, the use of nanotechnology delivery systems can reduce the required dosage, further making peptide therapy a sustainable option for neglected diseases, including leishmaniasis. Full article
(This article belongs to the Special Issue Antimicrobial Peptides as Promising Therapeutic Agents)
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23 pages, 3339 KB  
Article
Serendipitous Hinge Modulation Hypothetically Reprograms Caerin 1.1-LC Antibacterial Mechanism and Gram-Negative Selectivity
by Zhengze Sun, Ruixin Zhao, Yueao Zhang, Xiaonan Ma, Yangyang Jiang, Tao Wang, Xiaoling Chen, Chengbang Ma, Tianbao Chen, Chris Shaw, Mei Zhou and Lei Wang
Pharmaceutics 2025, 17(11), 1500; https://doi.org/10.3390/pharmaceutics17111500 - 20 Nov 2025
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Abstract
Background: The golden era of antibiotics has long passed, and the clinical failures caused by emerging drug-resistant bacteria have intensified the demand for novel antimicrobial agents. Antimicrobial peptides have attracted significant attention as promising candidates for next-generation antibiotics. Methods: In this study, we [...] Read more.
Background: The golden era of antibiotics has long passed, and the clinical failures caused by emerging drug-resistant bacteria have intensified the demand for novel antimicrobial agents. Antimicrobial peptides have attracted significant attention as promising candidates for next-generation antibiotics. Methods: In this study, we identified a novel antimicrobial peptide, Caerin 1.1-LC, from the skin secretion of the Australian green tree frog, Litoria caerulea. Subsequent structure–activity relationship studies led us to design a series of analogues and revealed the critical role of the peptide’s intrinsic hinge structure in shaping its biological activity. Results: Incorporation of D-isomers at the valine residues within the hinge preserved overall helical content but altered the hinge conformation, resulting in an 8-fold increase in antibacterial activity against Gram-negative bacteria. Simultaneously, haemolytic activity was markedly reduced, leading to a 56-fold improvement in therapeutic index (from 0.47 to 26.6). Structural modulation of the hinge also switched the mechanism of action from classical membrane disruption with associated permeability changes to a non-membrane-permeabilising, ‘cell-penetrating-like’ behaviour, inducing membrane potential depolarisation and ATP disruption to trigger bacterial death. In vivo studies using infected larval models, along with in vitro LPS neutralisation assays, further demonstrated the therapeutic potential of the D-analogue as a novel antibacterial agent. Conclusions: This work highlights the pivotal role of hinge structures in Caerin-family/hinge-containing AMPs, offering a strategic avenue for optimising antibacterial efficacy. Full article
(This article belongs to the Special Issue Antimicrobial Peptides as Promising Therapeutic Agents)
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Review

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38 pages, 8327 KB  
Review
Functional Peptides: Comparing Synthetic and Sequence-Engineered Antibiofilm Pharmaceutics
by Bilal Aslam, Muhammad Hassan Khalid and Sulaiman F. Aljasir
Pharmaceutics 2026, 18(4), 441; https://doi.org/10.3390/pharmaceutics18040441 - 2 Apr 2026
Viewed by 791
Abstract
Biofilm formation is a complex phenomenon employed by microbes to counteract antimicrobials. Biofilm-associated infections are a challenging threat to modern medicine. Antimicrobial peptides (AMPs) are recognized as some of the most promising therapeutics to tackle biofilm-producing and multidrug-resistant (MDR) pathogens. However, stability, toxicity, [...] Read more.
Biofilm formation is a complex phenomenon employed by microbes to counteract antimicrobials. Biofilm-associated infections are a challenging threat to modern medicine. Antimicrobial peptides (AMPs) are recognized as some of the most promising therapeutics to tackle biofilm-producing and multidrug-resistant (MDR) pathogens. However, stability, toxicity, and potency are key issues in the case of naturally occurring AMPs. Next-generation antibiofilm tools, such as synthetic or engineered AMPs, have emerged as a potent therapeutic choice. Synthetic peptides offer structural simplicity, versatility for chemical modification, and increased stability, which makes them capable of effectively disrupting both the biofilm matrix and the bacterial membrane. For engineered peptides, rational sequence modification, hybridization, and computational design are used to overcome limitations related to selectivity, biofilm-specific targeting and regulatory pathway modulation. This review provides a critical evaluation of synthetic and engineered AMPs from various perspectives, such as design strategies, antibiofilm action mechanisms, therapeutic performance, and translational potential. This study sheds light on current advances and emerging technologies, including AI-guided peptide optimization and multifunctional peptide platforms, and thereby sets the stage for the rational development of peptide-based therapeutics aimed at overcoming biofilm-mediated antimicrobial resistance (AMR). Full article
(This article belongs to the Special Issue Antimicrobial Peptides as Promising Therapeutic Agents)
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