Antimicrobial Peptides (AMPs) Against Human Pathogens

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

Deadline for manuscript submissions: 31 January 2027 | Viewed by 2135

Special Issue Editor


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Guest Editor
Laboratory of Bioinformatics Applied to Human Health, Center for Drug Research and Development (NPDM), Federal University of Ceará, Fortaleza 60355-636, Brazil
Interests: antimicrobial peptides (AMPs); molecular biology; synthetic and bioengineered peptide; biochemistry and virology
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Special Issue Information

Dear Colleagues,

Antimicrobial peptides (AMPs) have emerged as one of the most promising alternatives to conventional antibiotics in the fight against human pathogens. These naturally occurring molecules exhibit broad-spectrum activity against bacteria, viruses, fungi, and parasites, often with unique mechanisms that reduce the likelihood of resistance development. Beyond their direct antimicrobial effects, AMPs can also modulate the immune response, promote wound healing, and influence microbiome balance, making them highly versatile therapeutic candidates.

This Special Issue will bring together cutting-edge research and reviews focused on the discovery, design, and application of AMPs against clinically relevant pathogens. We particularly welcome contributions addressing novel mechanisms of action, structure–function relationships, synthetic and bioengineered peptide strategies, delivery systems, clinical trials, and the role of AMPs in overcoming antimicrobial resistance.

By providing a platform for interdisciplinary discussion, this Special Issue aims to highlight recent advances in AMP research and inspire innovative approaches toward their translation into effective therapies for human health.

We look forward to receiving your contributions.

Dr. Pedro Souza
Guest Editor

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Keywords

  • antimicrobial peptides (AMPs)
  • mechanisms
  • structure–function relationships
  • synthetic and bioengineered peptides

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Published Papers (2 papers)

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Research

12 pages, 2335 KB  
Communication
The Antimicrobial Peptide C14R Is Active Against All Pathogenic Species of the ESKAPE Group
by Daniel Gruber, Verena Vogel, Jan-Christoph Walter, Grigory Bolotnikov, Armando Rodríguez, Nico Preising, Ludger Ständker, Carolina Firacative, Barbara Spellerberg, Ann-Kathrin Kissmann and Frank Rosenau
Antibiotics 2026, 15(2), 211; https://doi.org/10.3390/antibiotics15020211 - 15 Feb 2026
Viewed by 1017
Abstract
The global rise in antimicrobial resistance among the ESKAPE pathogens represents a major challenge to public health. Here, we report the broad-spectrum antibacterial activity of the synthetic antimicrobial and pore-forming peptide C14R against all six ESKAPE species. Using a radial diffusion assay and [...] Read more.
The global rise in antimicrobial resistance among the ESKAPE pathogens represents a major challenge to public health. Here, we report the broad-spectrum antibacterial activity of the synthetic antimicrobial and pore-forming peptide C14R against all six ESKAPE species. Using a radial diffusion assay and resazurin-based viability testing, C14R exhibited a potent bactericidal effect with minimum inhibitory concentrations (MICs), defined as the lowest concentration of an antimicrobial agent that completely inhibits visible growth of planktonic microorganisms, ranging from 3.4 µg/mL (Enterococcus faecium, vancomycin-resistant) to 45.2 µg/mL (Klebsiella quasipneumoniae, ESBL). C14R also inhibited biofilm formation by Gram-positive pathogens, with minimum biofilm inhibitory concentrations (MBICs), referring to the minimal concentration required to prevent the development of biofilms, of 15.0 µg/mL (Staphylococcus aureus, MRSA) and 22.0 µg/mL (E. faecium, VRE), whereas Gram-negative biofilms showed higher tolerance. Together, these findings demonstrate that C14R retains high activity against multidrug-resistant ESKAPE strains, highlighting its potential as a lead compound for the development of next-generation antimicrobial drugs to expand the portfolio of available antibiotics and brace health systems against emerging severe infections. Full article
(This article belongs to the Special Issue Antimicrobial Peptides (AMPs) Against Human Pathogens)
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15 pages, 1182 KB  
Article
DVL, a Lectin from Dioclea violacea Seeds, Disturbs the Proteomic Profile of Candida krusei, Leading to Cell Death
by Romério R. S. Silva, Rayara J. P. Carvalho, Maria H. C. Santos, Ana L. E. Santos, Rômulo F. Carneiro, Celso S. Nagano, Pedro F. N. Souza and Claudener S. Teixeira
Antibiotics 2025, 14(12), 1228; https://doi.org/10.3390/antibiotics14121228 - 5 Dec 2025
Cited by 1 | Viewed by 834
Abstract
Background/Objectives Plant lectins have emerged as potential antifungal molecules, where the carbohydrate recognition domain (CRD) is possibly the main mode of action of these proteins. Previously, we saw that the lectin extracted from the seeds of Dioclea violacea (DVL) has anti-candida activity against [...] Read more.
Background/Objectives Plant lectins have emerged as potential antifungal molecules, where the carbohydrate recognition domain (CRD) is possibly the main mode of action of these proteins. Previously, we saw that the lectin extracted from the seeds of Dioclea violacea (DVL) has anti-candida activity against Candida krusei cells by acting to inhibit ergosterol biosynthesis, cell wall deformation, and deregulation of the redox system. Methods We have now confirmed this anti-candida activity by proteomic analysis, with the expression of proteins that show us how C. krusei cells respond to this treatment. Results A total of 395 proteins were identified: 142 proteins exclusively found in untreated C. krusei cells and 245 proteins exclusive to DVL-treated cells. Eight proteins were detected in both conditions. Six displayed positive accumulation (fold change > 1.5), one exhibited negative accumulation (fold change < 0.5). We observed the expression of proteins related to cell wall remodeling; alteration of energy metabolism, suggesting a metabolic adaptation to stress; oxidative stress was responded to through the expression of proteins with antioxidant action, in addition to identifying multidrug transport proteins that are often involved in the process of antifungal resistance and sterol transport to the membrane. Conclusions Our results show the complexity of adaptive responses of C. krusei cells to treatment with DVL, elucidating new mechanisms of resistance and paving the way for the development of more effective and innovative antifungal therapies. Full article
(This article belongs to the Special Issue Antimicrobial Peptides (AMPs) Against Human Pathogens)
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