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Antibiotics
Special Issues
Antimicrobial Activity of Bioactive Peptides and Their Derivatives
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Antimicrobial Activity of Bioactive Peptides and Their Derivatives

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

Deadline for manuscript submissions: 20 July 2025 | Viewed by 8377

Special Issue Editor

Dr. Alexandro Rodríguez-Rojas

E-Mail Website
Guest Editor
Department for Small Animal Internal Medicine, Clinic for Small Animals, University of Veterinary Medicine, Vienna, Austria
Interests: antimicrobial peptides; antimicrobials; host-pathogen interaction; infectious diseases; antimicrobial mechanism of action; bacterial genetics

Special Issue Information

Dear Colleagues,

The emergence and rapid spread of antimicrobial-resistant (AMR) microorganisms pose a significant global health threat. In the face of this growing challenge, there is an urgent need for novel antimicrobial agents with effective and broad-spectrum activity. Bioactive peptides (AMPs) represent a promising new class of antimicrobials that offer several advantages over traditional antibiotics. AMPs are naturally occurring peptides in various organisms, including humans, animals, plants, and microbes. They exhibit a broad spectrum of activity against several pathogens, including bacteria, fungi, and viruses.

Additionally, AMPs are less prone to developing resistance than traditional antibiotics. This Special Issue of Antibiotics will focus on the latest research on the antimicrobial activity of bioactive peptides and their derivatives. The issue will include articles on novel AMPs or their derivatives with potent antimicrobial activity, mechanisms of action of AMPs, structure–activity relationships of AMPs, development of AMP-based therapeutics, clinical applications of AMPs, and combinatory therapy with other antimicrobials.

Dr. Alexandro Rodríguez-Rojas
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 100 words) can be sent to the Editorial Office for announcement on this website.

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 resistance (AMR)
  • global health threat
  • novel antimicrobial agents
  • bioactive peptides (AMPs)
  • natural antimicrobial agents
  • broad-spectrum activity
  • antimicrobial activity
  • mechanisms of action
  • structure–activity relationships
  • AMP-based therapeutics
  • clinical applications of AMPs
  • combinatory therapy

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Further information on MDPI's Special Issue policies can be found here.

Published Papers (6 papers)

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Research

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21 pages, 8258 KiB  
Article
Structural Characterization of the Dimers and Selective Synthesis of the Cyclic Analogues of the Antimicrobial Peptide Cm-p5
by Fidel E. Morales-Vicente, Luis A. Espinosa, Erbio Díaz-Pico, Ernesto M. Martell, Melaine Gonzalez, Gerardo Ojeda, Luis Javier González, Armando Rodríguez, Hilda E. Garay, Octavio L. Franco, Frank Rosenau, Anselmo J. Otero-González and Ludger Ständker
Antibiotics 2025, 14(2), 194; https://doi.org/10.3390/antibiotics14020194 - 13 Feb 2025
Viewed by 765
Abstract
Background/Objectives: Cm-p5 and its cyclic monomeric and dimeric analogues are known for their antifungal, antibacterial, antiviral, and antibiofilm activities. Previously, our cyclization method produced a mixture of peptides that were difficult to separate, which was then improved by a selective synthesis of [...] Read more.
Background/Objectives: Cm-p5 and its cyclic monomeric and dimeric analogues are known for their antifungal, antibacterial, antiviral, and antibiofilm activities. Previously, our cyclization method produced a mixture of peptides that were difficult to separate, which was then improved by a selective synthesis of the parallel dimer and its differentiation from the antiparallel by comparison of the retention times in RP-HPLC. Methods: Here, we developed a more reliable identification method for the Cm-p5 dimer identification, which included chymotrypsin proteolytic digestion and sequencing of the different fragments by ESI-MSMS. We also improved our cyclization methods to specifically produce higher amounts of the desired cyclic variant, either cyclic monomer or dimer. Results: We show that liquid phase oxidation with 20% DMSO or iodine oxidation yields only the cyclic analogue. However, the on-resin oxidation with iodine showed greater efficacy and efficiency. Additionally, liquid phase cyclization yields the antiparallel dimer in high EtOH or peptide concentration, indicating a kinetic control. On the other hand, the parallel dimer was preferentially produced in 5% of TFE and low peptide concentration without the formation of the cyclic analogue indicating a thermodynamic control. Conclusions: In conclusion, we report that chymotryptic digestion combined with ESI-MS and MS/MS allows an unambiguous differentiation of Cm-p5 dimers. Here, we develop more selective and efficient methods for the synthesis of cyclic and dimeric analogues of Cm-p5. Full article
(This article belongs to the Special Issue Antimicrobial Activity of Bioactive Peptides and Their Derivatives)
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16 pages, 2974 KiB  
Article
PA-Win2: In Silico-Based Discovery of a Novel Peptide with Dual Antibacterial and Anti-Biofilm Activity
by Jin Wook Oh, Min Kyoung Shin, Hye-Ran Park, Sejun Kim, Byungjo Lee, Jung Sun Yoo, Won-Jae Chi and Jung-Suk Sung
Antibiotics 2024, 13(12), 1113; https://doi.org/10.3390/antibiotics13121113 - 21 Nov 2024
Viewed by 1253
Abstract
Background: The emergence and prevalence of antibiotic-resistant bacteria (ARBs) have become a serious global threat, as the morbidity and mortality associated with ARB infections are continuously rising. The activation of quorum sensing (QS) genes can promote biofilm formation, which contributes to the acquisition [...] Read more.
Background: The emergence and prevalence of antibiotic-resistant bacteria (ARBs) have become a serious global threat, as the morbidity and mortality associated with ARB infections are continuously rising. The activation of quorum sensing (QS) genes can promote biofilm formation, which contributes to the acquisition of drug resistance and increases virulence. Therefore, there is an urgent need to develop new antimicrobial agents to control ARB and prevent further development. Antimicrobial peptides (AMPs) are naturally occurring defense molecules in organisms known to suppress pathogens through a broad range of antimicrobial mechanisms. Methods: In this study, we utilized a previously developed deep-learning model to identify AMP candidates from the venom gland transcriptome of the spider Pardosa astrigera, followed by experimental validation. Results: PA-Win2 was among the top-scoring predicted peptides and was selected based on physiochemical features. Subsequent experimental validation demonstrated that PA-Win2 inhibits the growth of Bacillus subtilis, Escherichia coli, Staphylococcus aureus, Staphylococcus epidermidis, Pseudomonas aeruginosa, and multidrug-resistant P. aeruginosa (MRPA) strain CCARM 2095. The peptide exhibited strong bactericidal activity against P. aeruginosa, and MRPA CCARM 2095 through the depolarization of bacterial cytoplasmic membranes and alteration of gene expression associated with bacterial survival. In addition, PA-Win2 effectively inhibited biofilm formation and degraded pre-formed biofilms of P. aeruginosa. The gene expression study showed that the peptide treatment led to the downregulation of QS genes in the Las, Pqs, and Rhl systems. Conclusions: These findings suggest PA-Win2 as a promising drug candidate against ARB and demonstrate the potential of in silico methods in discovering functional peptides from biological data. Full article
(This article belongs to the Special Issue Antimicrobial Activity of Bioactive Peptides and Their Derivatives)
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13 pages, 1384 KiB  
Article
Anti-Biofilm and Anti-Inflammatory Properties of the Truncated Analogs of the Scorpion Venom-Derived Peptide IsCT against Pseudomonas aeruginosa
by Pornpimon Jantaruk, Kittitat Teerapo, Supattra Charoenwutthikun, Sittiruk Roytrakul and Duangkamol Kunthalert
Antibiotics 2024, 13(8), 775; https://doi.org/10.3390/antibiotics13080775 - 16 Aug 2024
Viewed by 1903
Abstract
Pseudomonas aeruginosa is an opportunistic pathogen in humans and a frequent cause of severe nosocomial infections and fatal infections in immunocompromised individuals. Its ability to form biofilms has been the main driving force behind its resistance to almost all conventional antibiotics, thereby limiting [...] Read more.
Pseudomonas aeruginosa is an opportunistic pathogen in humans and a frequent cause of severe nosocomial infections and fatal infections in immunocompromised individuals. Its ability to form biofilms has been the main driving force behind its resistance to almost all conventional antibiotics, thereby limiting treatment efficacy. In an effort to discover novel therapeutic agents to fight P. aeruginosa-associated biofilm infections, the truncated analogs of scorpion venom-derived peptide IsCT were synthesized and their anti-biofilm properties were examined. Among the investigated peptides, the IsCT-Δ6-8 peptide evidently showed the most potential anti-P. aeruginosa biofilm activity and the effect was not due to bacterial growth inhibition. The IsCT-Δ6-8 peptide also exhibited inhibitory activity against the production of pyocyanin, an important virulence factor of P. aeruginosa. Furthermore, the IsCT-Δ6-8 peptide significantly suppressed the production of inflammatory mediators nitric oxide and interleukin-6 in P. aeruginosa LPS-induced macrophages. Due to its low cytotoxicity to mammalian cells, the IsCT-Δ6-8 peptide emerges as a promising candidate with significant anti-biofilm and anti-inflammatory properties. These findings highlight its potential application in treating P. aeruginosa-related biofilm infections. Full article
(This article belongs to the Special Issue Antimicrobial Activity of Bioactive Peptides and Their Derivatives)
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11 pages, 1689 KiB  
Article
A Cyclic Peptide Based on Pheasant Cathelicidin Inhibits Influenza A H1N1 Virus Infection
by Yaping Pei, Zhihua Chen, Ruihan Zhao, Yanxing An, Haiche Yisihaer, Chaojie Wang, Yaning Bai, Libin Liang, Lin Jin and Yongting Hu
Antibiotics 2024, 13(7), 606; https://doi.org/10.3390/antibiotics13070606 - 28 Jun 2024
Viewed by 1272
Abstract
Influenza viruses are the leading cause of upper respiratory tract infections, leading to several global pandemics and threats to public health. Due to the continuous mutation of influenza A viruses, there is a constant need for the development of novel antiviral therapeutics. Recently, [...] Read more.
Influenza viruses are the leading cause of upper respiratory tract infections, leading to several global pandemics and threats to public health. Due to the continuous mutation of influenza A viruses, there is a constant need for the development of novel antiviral therapeutics. Recently, natural antimicrobial peptides have provided an opportunity for the discovery of anti-influenza molecules. Here, we designed several peptides based on pheasant cathelicidin and tested their antiviral activities and mechanisms against the H1N1 virus. Of note, the designed peptides Pc-4 and Pc-5 were found to inhibit replication of the H1N1 virus with an IC50 = 8.14 ± 3.94 µM and 2.47 ± 1.95 µM, respectively. In addition, the cyclic peptide Pc-5 was found to induce type I interferons and the expression of interferon-induced genes. An animal study showed that the cyclic peptide Pc-5 effectively inhibited H1N1 virus infection in a mouse model. Taken together, our work reveals a strategy for designing cyclic peptides and provides novel molecules with therapeutic potential against influenza A virus infection. Full article
(This article belongs to the Special Issue Antimicrobial Activity of Bioactive Peptides and Their Derivatives)
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11 pages, 3242 KiB  
Article
Efficacy of Short Novel Antimicrobial Peptides in a Mouse Model of Staphylococcus pseudintermedius Skin Infection
by Mingyu Ouyang, Fangrong Wu and Changmin Hu
Antibiotics 2024, 13(6), 508; https://doi.org/10.3390/antibiotics13060508 - 30 May 2024
Viewed by 1795
Abstract
As the clinical application of antibiotics for bacterial skin infections in companion animals becomes increasingly prevalent, the issue of bacterial resistance has become more pronounced. Antimicrobial peptides, as a novel alternative to traditional antibiotics, have garnered widespread attention. In our study, synthetic peptides [...] Read more.
As the clinical application of antibiotics for bacterial skin infections in companion animals becomes increasingly prevalent, the issue of bacterial resistance has become more pronounced. Antimicrobial peptides, as a novel alternative to traditional antibiotics, have garnered widespread attention. In our study, synthetic peptides ADD-A and CBD3-ABU were tested against Staphylococcus pseudintermedius skin infections in KM mice. ADD-A was applied topically and through intraperitoneal injection, compared with control groups and treatments including CBD3-ABU, ampicillin sodium, and saline. Wound contraction, bacterial counts and histology were assessed on days 3 and 11 post-infection. ADD-A and ampicillin treatments significantly outperformed saline in wound healing (p < 0.0001 and p < 0.001, respectively). ADD-A also showed a markedly lower bacterial count than ampicillin (p < 0.0001). Histologically, ADD-A-applied wounds had better epidermal continuity and a thicker epidermis than normal, with restored follicles and sebaceous glands. ADD-A’s effectiveness suggests it as a potential alternative to antibiotics for treating skin infections in animals. Full article
(This article belongs to the Special Issue Antimicrobial Activity of Bioactive Peptides and Their Derivatives)
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Review

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17 pages, 1481 KiB  
Review
Bacterial Extracellular Vesicles and Antimicrobial Peptides: A Synergistic Approach to Overcome Antimicrobial Resistance
by Corina Ciobanasu
Antibiotics 2025, 14(4), 414; https://doi.org/10.3390/antibiotics14040414 - 19 Apr 2025
Viewed by 512
Abstract
Antimicrobial resistance is already a major global health threat, contributing to nearly 5 million deaths annually. The rise of multidrug-resistant pathogens has made many infections increasingly difficult to treat. This growing threat has driven the search for alternative therapeutic approaches. Among the most [...] Read more.
Antimicrobial resistance is already a major global health threat, contributing to nearly 5 million deaths annually. The rise of multidrug-resistant pathogens has made many infections increasingly difficult to treat. This growing threat has driven the search for alternative therapeutic approaches. Among the most promising candidates are bacterial extracellular vesicles (BEVs) and antimicrobial peptides (AMPs), which offer unique mechanisms of action, potential synergistic effects, and the ability to bypass conventional resistance pathways. This review summarizes the current research on synergistic effects of BEVs and AMPs to overcome antimicrobial resistance. Full article
(This article belongs to the Special Issue Antimicrobial Activity of Bioactive Peptides and Their Derivatives)
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