Antimicrobial Peptides: Design, Synthesis and Pharmaceutical Applications

A special issue of Pharmaceuticals (ISSN 1424-8247). This special issue belongs to the section "Biopharmaceuticals".

Deadline for manuscript submissions: closed (25 October 2024) | Viewed by 1624

Special Issue Editor


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Guest Editor
Department of Biochemistry, School of Medicine, Tzu Chi University, Hualien 97004, Taiwan
Interests: antimicrobial peptides; computational structural biochemistry; protein and peptide engineering; nano-biomaterials; bacteriology and virology

Special Issue Information

Dear Colleagues,

Natural functional peptides have been identified in a wide range of organisms, exhibiting a variety of functions including antibiotic/antifungal/antiviral, anticancer, cardiovascular, gastrointestinal, neurochemical, renal, respiratory, and immune/inflammatory functions. As they can be easily modified in their amino acid sequences, and synthesized chemically using relatively straightforward methods, therapeutic peptides have drawn great attention as candidates for drug developments. Currently, clinical practice is facing problems caused by the rapid development of antibiotic resistance in bacteria. Most of the traditional antibiotics used in routine treatments for bacterial infections are losing their efficacies. As a result, there is an urgent need to continually develop novel effective antibiotics to be used in clinical practice. For this purpose, a group of peptide-based pharmaceuticals, antimicrobial peptides, have emerged as the focus of various studies. Intensive and extensive efforts have been made in this field by research scientists around the world, and a large number of antimicrobial peptides have been yielded, of which some have been successfully marketed and many are under development in different stages. Many of the antimicrobial peptides have been demonstrated to exhibit broad-spectrum antimicrobial activities against different types of pathogens. A number of antimicrobial peptides have also been found to alter host immuno and inflammatory responses to pathogen infections.  As antimicrobial peptides adopt different bactericidal mechanisms from those of traditional antibiotics, they are less prone to resistance development in bacteria. However, there are also challenges associated with the use of antimicrobial peptides, such as stability issues, mammalian cytotoxicity and hemolysis, cost of production, and potential immunogenicity, etc. Therefore, research is required on addressing these issues to harness the full therapeutic potential of antimicrobial peptides.

This Special Issue entitled “Antimicrobial Peptides: Design, Synthesis and Pharmaceutical Applications” aims to publish original research and review articles related to all aspects of antimicrobial peptides, including peptide design, modifications, identifications, synthesis, stability, interactions with bacterial components, and clinical applications, etc. Papers on the effects of peptides on inflammatory responses in infected hosts, and the extended applications or repurposing of antimicrobial peptides to treat cancers and other diseases are also within the scope of this Special Issue.

Prof. Dr. Je-Wen Liou
Guest Editor

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Keywords

  • natural antimicrobial peptides
  • antimicrobial peptide design and modifications
  • antimicrobial peptide structures
  • antimicrobial peptide stability
  • mechanism/mode of action of antimicrobial peptides
  • antimicrobial peptide applications
  • modulation of infection-related immune and inflammation by peptides
  • extended applications of antimicrobial peptides for treatments of cancers and other diseases
  • clinical trials of pharmaceutical peptides

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Published Papers (1 paper)

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Research

21 pages, 7637 KiB  
Article
Study of Potential Blocking Peptides Targeting the SARS-CoV-2 RBD/hACE2 Interaction
by Sara M. Villada-Troncoso, Jenny Andrea Arévalo-Romero, Vanessa Hernández Rivera, Martha Pedraza-Escalona, Sonia M. Pérez-Tapia, Angela Johana Espejo-Mojica and Carlos Javier Alméciga-Díaz
Pharmaceuticals 2024, 17(9), 1240; https://doi.org/10.3390/ph17091240 - 20 Sep 2024
Viewed by 1289
Abstract
Background/Objectives: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of COVID-19, was declared a public health emergency in early 2020. The infection initiates when the receptor-binding domain (RBD) of the viral spike protein binds to human angiotensin-converting enzyme 2 (ACE2). Despite [...] Read more.
Background/Objectives: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of COVID-19, was declared a public health emergency in early 2020. The infection initiates when the receptor-binding domain (RBD) of the viral spike protein binds to human angiotensin-converting enzyme 2 (ACE2). Despite the success of vaccination efforts, the emergence of new variants highlights the ongoing need for treatments targeting these evolving strains. In silico methods previously identified peptides BP2, BP9, and BP11 as being capable of disrupting the RBD-ACE2 interaction, though their efficacy has not been experimentally validated until now. Methods: In this study, these peptides were recombinantly produced in the yeast Komagataella phaffii, and the activity was assessed in vitro using binding assays with multiple RBD variants and the inhibition of the RBD-ACE2 interaction. Results: The production yield for BP2, BP9, and BP11 was 14.34, 4.01, and 1.35 mg per culture liter, respectively. Noteworthy, the three BPs interacted with the RBD of SARS-CoV-2 variants of concern, with BP2 showing higher recognition. Finally, the BPs showed an RBD/hACE2 interaction blocking capacity with IC50 values between 1.03 and 5.35 nM, with BP2 showing the lowest values among the evaluated peptides. Conclusions: These results demonstrate that BP2, specifically, is a promising candidate for the development of novel therapeutic interventions targeting SARS-CoV-2 and other coronaviruses that use hACE2 for cellular entry. Full article
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