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Antimicrobial and Antiviral Peptides
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Antimicrobial and Antiviral Peptides

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pharmacology".

Deadline for manuscript submissions: closed (20 March 2025) | Viewed by 18151

Special Issue Editor

Dr. Tecla Ciociola

E-Mail Website
Guest Editor
Department of Medicine and Surgery, University of Parma, 43126 Parma, Italy
Interests: antimicrobial peptides; serum protein-derived peptides; infectious diseases; anti-infective peptides; anti-biofilm peptides; structure–activity relationship of peptides; in silico analysis
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Infectious diseases still constitute a major problem for public health in relation to the emergence of resistance against conventional antiinfective drugs. It is therefore necessary to identify new therapeutic strategies against infections. In the last twenty years, peptides have experienced a revival as potential therapeutic drugs thanks to new chemical synthesis procedures and the nano-delivery technologies applied in the peptide field.

This Special Issue aims to highlight the recent research in the field of antimicrobial and antiviral peptides. This includes, but is not limited to, (i) identification of novel natural, synthetic or in silico-designed peptides, (ii) functional and structural characterization and structure–function relationships, (iii) identification of molecular targets and (iv) possible biomedical applications.

Since International Journal of Molecular Sciences is a journal of molecular science, pure clinical studies will not be suitable for the journal. However, clinical submissions with biomolecular experiments are welcomed.

Dr. Tecla Ciociola
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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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
  • antiviral peptides
  • peptide mining
  • molecular mechanism of biological activity
  • structure–activity relationship
  • molecular targets
  • in silico design
  • in vivo models
  • peptide delivery strategies
  • biomedical applications

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Published Papers (7 papers)

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Research

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16 pages, 3792 KiB  
Article
The Role of Temperature and Subphase Components in Shaping Selected Physicochemical Properties of the Phosphatidylinositol Monolayer
by Iwona Golonka, Izabela W. Łukasiewicz, Aleksandra Sebastiańczyk, Katarzyna E. Greber, Wiesław Sawicki and Witold Musiał
Int. J. Mol. Sci. 2025, 26(8), 3472; https://doi.org/10.3390/ijms26083472 - 8 Apr 2025
Viewed by 383
Abstract
Acne vulgaris is one of the most common skin diseases, and its development is closely linked to the overgrowth of the bacterium Cutibacterium acnes. More than half of the strains of this bacterium are resistant to antibiotics, which has prompted scientists to [...] Read more.
Acne vulgaris is one of the most common skin diseases, and its development is closely linked to the overgrowth of the bacterium Cutibacterium acnes. More than half of the strains of this bacterium are resistant to antibiotics, which has prompted scientists to look for alternatives, such as antibacterial peptides, that can replace traditional drugs. Due to its antioxidant properties, ascorbic acid may be a promising ally in the treatment of acne. The aim of our study was to evaluate the effect of peptide (KWK)2-KWWW-NH2(P5) in the presence of ascorbic acid (AA) and its derivative (3-O-ethyl-L-ascorbic acid, EAA) on the stability and organization of phosphatidylinositol monolayers (PI) at temperatures of 25–35 °C. This study showed that the monolayers were in the expanded liquid state (35.28–49.95 mN/m) or in the transition between the expanded liquid and condensed phases (51.50–57.49 mN/m). Compression and decompression isotherms indicated the highest flexibility of the PI + P5 system, where the compression reversibility coefficient of isotherm values ranged from 80.59% to 97.77% and increased for each loop with increasing temperature. At 35 °C, the surface pressure of the monolayer in the PI + P5, PI + P5 + AA and PI + P5 + EAA systems changed less with time. Full article
(This article belongs to the Special Issue Antimicrobial and Antiviral Peptides)
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11 pages, 4543 KiB  
Article
Antimicrobial Peptide CATH-2 Attenuates Avian Pathogenic E. coli-Induced Inflammatory Response via NF-κB/NLRP3/MAPK Pathway and Lysosomal Dysfunction in Macrophages
by Yating Xu, Liuyi Xu, Tingting Zhang, Hongliang Tian, Yi Lu, Sha Jiang, Xuefeng Cao, Zhiwei Li, Xiaoxiang Hu, Rendong Fang and Lianci Peng
Int. J. Mol. Sci. 2024, 25(23), 12572; https://doi.org/10.3390/ijms252312572 - 22 Nov 2024
Cited by 2 | Viewed by 1118
Abstract
Cathelicidins have anti-inflammatory activity and chicken cathelicidin-2 (CATH-2) has shown to modulate immune response, but the underlying mechanism of its anti-inflammation is still unclear. Therefore, in this study, we investigated the anti-inflammatory activity of CATH-2 on murine peritoneal macrophages during avian pathogenic E. [...] Read more.
Cathelicidins have anti-inflammatory activity and chicken cathelicidin-2 (CATH-2) has shown to modulate immune response, but the underlying mechanism of its anti-inflammation is still unclear. Therefore, in this study, we investigated the anti-inflammatory activity of CATH-2 on murine peritoneal macrophages during avian pathogenic E. coli (APEC) infection. The results showed that CATH-2 priming significantly reduced the production of IL-1β, IL-6, IL-1α, and IL-12. In addition, CATH-2 significantly attenuated APEC-induced caspase-1 activation and the formation of an adaptor (ASC) of NLRP3 inflammasome, indicating that CATH-2 inhibits APEC-induced NLRP3 inflammasome activation. Furthermore, CATH-2 remarkably inhibited NF-κB and MAPK signaling pathways activation. Moreover, CATH-2 significantly inhibited mRNA expression of cathepsin B and inhibited lysosomal acidification, demonstrating that CATH-2 disrupts lysosomal function. In addition, promoting lysosomal acidification using ML-SA1 hampered the anti-inflammatory effect of CATH-2 on APEC-infected cells. In conclusion, our study reveals that CATH-2 inhibits APEC-induced inflammation via the NF-κB/NLRP3/MAPK pathway through the dysfunction of lysosome. Full article
(This article belongs to the Special Issue Antimicrobial and Antiviral Peptides)
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13 pages, 1250 KiB  
Article
Anti-Herpetic Activity of Killer Peptide (KP): An In Vitro Study
by Arianna Sala, Francesco Ricchi, Laura Giovati, Stefania Conti, Tecla Ciociola and Claudio Cermelli
Int. J. Mol. Sci. 2024, 25(19), 10602; https://doi.org/10.3390/ijms251910602 - 1 Oct 2024
Cited by 2 | Viewed by 1372
Abstract
Antimicrobial peptides represent a promising alternative to traditional drugs in relation to cost, toxicity, and, primarily, the growing problem of drug resistance. Here, we report on the activity against HSV-1 and HSV-2 of a previously described wide-spectrum synthetic decapeptide, Killer Peptide (KP). As [...] Read more.
Antimicrobial peptides represent a promising alternative to traditional drugs in relation to cost, toxicity, and, primarily, the growing problem of drug resistance. Here, we report on the activity against HSV-1 and HSV-2 of a previously described wide-spectrum synthetic decapeptide, Killer Peptide (KP). As determined by plaque reduction assays, treatment with KP at 100 μg/mL resulted in a reduction in the viral yield titer of 3.5 Logs for HSV-1 and 4.1 Logs for HSV-2. Further evaluation of KP antiviral activity focused on the early stages of the virus replicative cycle, including the determination of the residual infectivity of viral suspensions treated with KP. A direct effect of the peptide on viral particles impairing virus absorption and penetration was shown. The toxicity profile proved to be extremely good, with a selectivity index of 29.6 for HSV-1 and 156 for HSV-2. KP was also active against acyclovir (ACV)-resistant HSV isolates, while HSV subcultures in the presence of sub-inhibitory doses of KP did not lead to the emergence of resistant strains. Finally, the antiviral action of KP proved to be synergistic with that of ACV. Overall, these results demonstrate that KP could represent an interesting addition/alternative to acyclovir for antiviral treatment. Full article
(This article belongs to the Special Issue Antimicrobial and Antiviral Peptides)
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16 pages, 2634 KiB  
Article
In Vitro Profiling of the Antiviral Peptide TAT-I24
by Theodhora Ziu, Ezgi Sambur, Zsolt Ruzsics, Hartmut Hengel, Reingard Grabherr, Siegfried Höfinger and Hanna Harant
Int. J. Mol. Sci. 2024, 25(19), 10463; https://doi.org/10.3390/ijms251910463 - 28 Sep 2024
Cited by 1 | Viewed by 4214
Abstract
The synthetic peptide TAT-I24 (GRKKRRQRRRPPQCLAFYACFC) exerts antiviral activity against several double-stranded (ds) DNA viruses, including herpes simplex viruses, cytomegalovirus, some adenoviruses, vaccinia virus and SV40 polyomavirus. In the present study, in vitro profiling of this peptide was performed with the aim of characterizing [...] Read more.
The synthetic peptide TAT-I24 (GRKKRRQRRRPPQCLAFYACFC) exerts antiviral activity against several double-stranded (ds) DNA viruses, including herpes simplex viruses, cytomegalovirus, some adenoviruses, vaccinia virus and SV40 polyomavirus. In the present study, in vitro profiling of this peptide was performed with the aim of characterizing and improving its properties for further development. As TAT-I24 contains three free cysteine residues, a potential disadvantageous feature, peptide variants with replacements or deletions of specific residues were generated and tested in various cell systems and by biochemical analyses. Some cysteine replacements had no impact on the antiviral activity, such as the deletion of cysteine 14, which also showed improved biochemical properties, while the cyclization of cysteines 14 and 20 had the most detrimental effect on antiviral activity. At concentrations below 20 µM, TAT-I24 and selected variants did not induce hemolysis in red blood cells (RBCs) nor modulated lipopolysaccharide (LPS)-induced release of cytokines, such as interleukin-6 (IL-6) and tumor necrosis factor-α (TNF-α), in human peripheral blood mononuclear cells (PBMCs). These data indicate that TAT-I24 or its peptide variants are not expected to cause unwanted effects on blood cells. Full article
(This article belongs to the Special Issue Antimicrobial and Antiviral Peptides)
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21 pages, 9651 KiB  
Article
Polymyxin B Peptide Hydrogel Coating: A Novel Approach to Prevent Ventilator-Associated Pneumonia
by Milan Wouters, Laurence Van Moll, Linda De Vooght, Emilia Choińska, Joanna Idaszek, Karol Szlązak, Marcin K. Heljak, Wojciech Święszkowski and Paul Cos
Int. J. Mol. Sci. 2024, 25(19), 10269; https://doi.org/10.3390/ijms251910269 - 24 Sep 2024
Cited by 1 | Viewed by 2034
Abstract
Ventilator-associated pneumonia (VAP) remains one of the most common hospital-acquired infections (HAI). Considering the complicated diagnosis and the lack of effective treatment, prophylactic measures are suggested as the new standard to prevent the disease. Although VAP often manifests a polymicrobial nature, Pseudomonas aeruginosa [...] Read more.
Ventilator-associated pneumonia (VAP) remains one of the most common hospital-acquired infections (HAI). Considering the complicated diagnosis and the lack of effective treatment, prophylactic measures are suggested as the new standard to prevent the disease. Although VAP often manifests a polymicrobial nature, Pseudomonas aeruginosa remains one of the pathogens associated with the highest morbidity and mortality rates within these mechanically ventilated patients. In this paper, we report on the development of an antibacterial hydrogel coating using the polymyxin B (PMB) peptide to prevent bacterial adhesion to the polymeric substrate. We fully characterized the properties of the coating using atomic force microscopy (AFM), scanning electron microscopy (SEM), wettability analyses and Fourier-transform infrared (FTIR) and Raman spectroscopy. Furthermore, several biological assays confirmed the antibacterial and anti-biofilm effect of the tubing for at least 8 days against P. aeruginosa. On top of that, the produced coating is compliant with the requirements regarding cytocompatibility stated in the ISO (International Organization for Standardization) 10993 guidelines and an extended release of PMB over a period of at least 42 days was detected. In conclusion, this study serves as a foundation for peptide-releasing hydrogel formulas in the prevention of VAP. Full article
(This article belongs to the Special Issue Antimicrobial and Antiviral Peptides)
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13 pages, 2925 KiB  
Article
Optimization and Stability Assessment of Monochamus alternatus Antimicrobial Peptide MaltAtt-1 in Komagataella phaffii GS115 for the Control of Pine Wood Nematode
by Di Jiang, Xuhuizi Xu, Zeguang Wang, Chao Yu, Zeqing Wang, Yuda Xu, Xu Chu, Ming Li, Feiping Zhang and Xia Hu
Int. J. Mol. Sci. 2024, 25(16), 8555; https://doi.org/10.3390/ijms25168555 - 6 Aug 2024
Viewed by 1316
Abstract
MaltAtt-1 is an antimicrobial peptide isolated from Monochamus alternatus with nematocidal activity against pine wood nematode. In this study, a eukaryotic expression system based on Komagataella phaffii GS115 was established, and its secretory expression of MaltAtt-1 was realized. The basic properties and secondary and [...] Read more.
MaltAtt-1 is an antimicrobial peptide isolated from Monochamus alternatus with nematocidal activity against pine wood nematode. In this study, a eukaryotic expression system based on Komagataella phaffii GS115 was established, and its secretory expression of MaltAtt-1 was realized. The basic properties and secondary and tertiary structures of the antimicrobial peptide MaltAtt-1 were identified by bioinformatics analysis. MaltAtt-1 is a hydrophilic stable protein, mainly composed of an α-helix (Hh), β-folds (Ee), and irregular curls (Cc). The optimal fermentation conditions for MaltAtt-1 were determined by a single-factor test and the Box–Behnken response surface method, including an induction time of 72 h, induction temperature of 30 °C, culture medium of pH 7.6, methanol volume fraction of 2.0%, and an initial glycerol concentration of 1%. The stability of MaltAtt-1 indicated its resistant to UV irradiation and repeated freezing and thawing, but the antibacterial activity decreased significantly under the influence of high temperature and a strong acid and base, and it decreased significantly to 1.1 cm and 0.83 cm at pH 2.0 and pH 10.0, respectively. The corrected mortality of B. xylophilus achieved 71.94% in 3 h at a concentration of 300 mg·L−1 MaltAtt-1 exposure. The results provide a theoretical basis for the antimicrobial peptide MaltAtt-1 to become a new green and efficient nematicide. Full article
(This article belongs to the Special Issue Antimicrobial and Antiviral Peptides)
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19 pages, 1652 KiB  
Review
Antimicrobial Peptides towards Clinical Application—A Long History to Be Concluded
by Laura Cresti, Giovanni Cappello and Alessandro Pini
Int. J. Mol. Sci. 2024, 25(9), 4870; https://doi.org/10.3390/ijms25094870 - 29 Apr 2024
Cited by 48 | Viewed by 6071
Abstract
Antimicrobial peptides (AMPs) are molecules with an amphipathic structure that enables them to interact with bacterial membranes. This interaction can lead to membrane crossing and disruption with pore formation, culminating in cell death. They are produced naturally in various organisms, including humans, animals, [...] Read more.
Antimicrobial peptides (AMPs) are molecules with an amphipathic structure that enables them to interact with bacterial membranes. This interaction can lead to membrane crossing and disruption with pore formation, culminating in cell death. They are produced naturally in various organisms, including humans, animals, plants and microorganisms. In higher animals, they are part of the innate immune system, where they counteract infection by bacteria, fungi, viruses and parasites. AMPs can also be designed de novo by bioinformatic approaches or selected from combinatorial libraries, and then produced by chemical or recombinant procedures. Since their discovery, AMPs have aroused interest as potential antibiotics, although few have reached the market due to stability limits or toxicity. Here, we describe the development phase and a number of clinical trials of antimicrobial peptides. We also provide an update on AMPs in the pharmaceutical industry and an overall view of their therapeutic market. Modifications to peptide structures to improve stability in vivo and bioavailability are also described. Full article
(This article belongs to the Special Issue Antimicrobial and Antiviral Peptides)
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