Antimicrobial Peptides and Their Potential Pharmaceutical Applications

A special issue of Pharmaceutics (ISSN 1999-4923). This special issue belongs to the section "Biopharmaceutics".

Deadline for manuscript submissions: 10 January 2025 | Viewed by 1117

Special Issue Editors


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Guest Editor
Pharmacy Programme, Department of Health Sciences, University of Nicosia, Nicosia, Cyprus
Interests: peptides; peptide synthesis; natural products; pharmacognosy
Special Issues, Collections and Topics in MDPI journals

E-Mail Website
Guest Editor
1. Department of Health Sciences, Pharmacy, University of Nicosia, 46 Makedonitissas Ave, P.O. Box 24005, 1700 Nicosia, Cyprus
2. Boactive Molecules Research Center, 46 Makedonitissas Ave, P.O. Box 24005, 1700 Nicosia, Cyprus
Interests: peptides; peptide synthesis; drug delivery; medicinal chemistry

Special Issue Information

Dear Colleagues,

The European Union and World Health Organisation have declared antimicrobial resistance among the major global public health threats facing humanity. Especially in the EU/EEA, it is reported to be responsible for more than 35,000 deaths every year. In addition, resistant microorganisms also have significant consequences, including for healthcare systems. Therefore, new therapeutic strategies are urgently needed.

Antimicrobial peptides (AMPs) play a critical role in the immune system and have distinctive structures and functions for sophisticated action mechanisms to kill or inhibit the growth of bacteria, fungi, parasites, viruses and cancer cells. Antibacterial peptides are critical and promising tools for antimicrobial drug development. This Special Issue aims to extend and update knowledge on the antimicrobial peptides and their potential pharmaceutical applications. Potential topics include, but are not limited to, the following: the screening of antimicrobial peptides, efficacy of novel antimicrobial peptides, mechanisms of action, stability and the ADME profile, the biological functions of antimicrobial peptides, in vivo studies and delivery strategies.

Original articles as well as reviews of studies on these topics are welcome.

Dr. Christos Petrou
Dr. Yiannis Sarigiannis
Dr. Christos Papaneophytou
Guest Editors

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Keywords

  • antimicrobial peptides in pharmaceutical applications
  • screening of antimicrobial peptides
  • efficacy of novel antimicrobial peptides
  • drug delivery
  • stability
  • ADME profile
  • biological functions of antimicrobial peptides
  • wound healing

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Published Papers (1 paper)

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Research

15 pages, 4197 KiB  
Article
Effective Immobilization of Novel Antimicrobial Peptides via Conjugation onto Activated Silicon Catheter Surfaces
by Irem Soyhan, Tuba Polat, Erkan Mozioglu, Tugba Arzu Ozal Ildenız, Merve Acikel Elmas, Sinan Cebeci, Nihan Unubol and Ozgul Gok
Pharmaceutics 2024, 16(8), 1045; https://doi.org/10.3390/pharmaceutics16081045 - 6 Aug 2024
Viewed by 837
Abstract
Antibiotic-resistant microorganisms have become a serious threat to public health, resulting in hospital infections, the majority of which are caused by commonly used urinary tract catheters. Strategies for preventing bacterial adhesion to the catheters’ surfaces have been potentially shown as effective methods, such [...] Read more.
Antibiotic-resistant microorganisms have become a serious threat to public health, resulting in hospital infections, the majority of which are caused by commonly used urinary tract catheters. Strategies for preventing bacterial adhesion to the catheters’ surfaces have been potentially shown as effective methods, such as coating thesurface with antimicrobial biomolecules. Here, novel antimicrobial peptides (AMPs) were designed as potential biomolecules to prevent antibiotic-resistant bacteria from binding to catheter surfaces. Thiolated AMPs were synthesized using solid-phase peptide synthesis (SPPS), and prep-HPLC was used to obtain AMPs with purity greater than 90%. On the other side, the silicone catheter surface was activated by UV/ozone treatment, followed by functionalization with allyl moieties for conjugation to the free thiol group of cystein in AMPs using thiol-ene click chemistry. Peptide-immobilized surfaces were found to become more resistant to bacterial adhesion while remaining biocompatible with mammalian cells. The presence and site of conjugation of peptide molecules were investigated by immobilizing them to catheter surfaces from both ends (C-Pep and Pep-C). It was clearly demonstrated that AMPs conjugated to the surface via theirN terminus have a higher antimicrobial activity. This strategy stands out for its effective conjugation of AMPs to silicone-based implant surfaces for the elimination of bacterial infections. Full article
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