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Peptide-Lead Drug Discovery
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Peptide-Lead Drug Discovery

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Medicinal Chemistry".

Deadline for manuscript submissions: closed (31 January 2020) | Viewed by 11809

Special Issue Editor

Prof. Dr. Hirokazu Tamamura

E-Mail Website
Guest Editor
Department of Medicinal Chemistry, Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University, Tokyo, Japan
Interests: medicinal chemistry; bioorganic chemistry; chemical biology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Peptides represent an attractive class of molecules for the design of new drugs, lead structures, drug carriers, and excepients. Recent developments in peptide synthesis techniques and high-throughput screening platforms have created enthusiasm and interest in the design and discovery of novel peptides for a broad range of biological and pharmacological applications. Advances in peptide engineering have helped to overcome traditional limitations in peptide drug development such as poor systemic stability, rapid clearance, and low binding affinities to biological targets. Currently, there are nearly one hundred peptide-based drug candidates in clinical trials, a dramatic increase compared to the number of those under study a decade ago. These developments signal a ‘second wave’ in peptide drug development.

Over the past decade, peptide drug discovery has experienced a revival of interest and scientific momentum, as the pharmaceutical industry has come to appreciate the role that peptide therapeutics can play in addressing unmet medical needs and how this class of compounds can be an excellent complement or even a preferable alternative to small-molecule and biological therapeutics.

This Special Issue of Molecules welcomes submissions of review and research articles in the field of peptide drug discovery and development.

Prof. Dr. Hirokazu Tamamura
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. Molecules is an international peer-reviewed open access semimonthly 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 2700 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

  • therapeutic peptides
  • peptide synthesis
  • drug development
  • drug targeting
  • antimicrobial peptides
  • peptides and Alzheimer disease
  • peptides and metabolic syndrome
  • peptides and cancer
  • peptides as shuttles
  • peptide-based drug delivery
  • peptide-based vaccines
  • peptides–drug conjugates

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Published Papers (3 papers)

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Research

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13 pages, 3926 KiB  
Article
Anti-Biofilm Effects of Synthetic Antimicrobial Peptides Against Drug-Resistant Pseudomonas aeruginosa and Staphylococcus aureus Planktonic Cells and Biofilm
by Seong-Cheol Park, Min-Young Lee, Jin-Young Kim, Hyeonseok Kim, Myunghwan Jung, Min-Kyoung Shin, Woo-Kon Lee, Gang-Won Cheong, Jung Ro Lee and Mi-Kyeong Jang
Molecules 2019, 24(24), 4560; https://doi.org/10.3390/molecules24244560 - 12 Dec 2019
Cited by 32 | Viewed by 4438
Abstract
Biofilm-associated infections are difficult to manage or treat as biofilms or biofilm-embedded bacteria are difficult to eradicate. Antimicrobial peptides have gained increasing attention as a possible alternative to conventional drugs to combat drug-resistant microorganisms because they inhibit the growth of planktonic bacteria by [...] Read more.
Biofilm-associated infections are difficult to manage or treat as biofilms or biofilm-embedded bacteria are difficult to eradicate. Antimicrobial peptides have gained increasing attention as a possible alternative to conventional drugs to combat drug-resistant microorganisms because they inhibit the growth of planktonic bacteria by disrupting the cytoplasmic membrane. The current study investigated the effects of synthetic peptides (PS1-2, PS1-5, and PS1-6) and conventional antibiotics on the growth, biofilm formation, and biofilm reduction of drug-resistant Pseudomonas aeruginosa and Staphylococcus aureus. The effects of PS1-2, PS1-5, and PS1-6 were also tested in vivo using a mouse model. All peptides inhibited planktonic cell growth and biofilm formation in a dose-dependent manner. They also reduced preformed biofilm masses by removing the carbohydrates, extracellular DNA, and lipids that comprised extracellular polymeric substances (EPSs) but did not affect proteins. In vivo, PS1-2 showed the greatest efficacy against preformed biofilms with no cytotoxicity. Our findings indicate that the PS1-2 peptide has potential as a next-generation therapeutic drug to overcome multidrug resistance and to regulate inflammatory response in biofilm-associated infections. Full article
(This article belongs to the Special Issue Peptide-Lead Drug Discovery)
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13 pages, 2818 KiB  
Article
NMR Study of the Secondary Structure and Biopharmaceutical Formulation of an Active Branched Antimicrobial Peptide
by Francesca Castiglia, Fabrizia Zevolini, Giulia Riolo, Jlenia Brunetti, Alessandra De Lazzari, Alberto Moretto, Giulia Manetto, Marco Fragai, Jenny Algotsson, Johan Evenäs, Luisa Bracci, Alessandro Pini and Chiara Falciani
Molecules 2019, 24(23), 4290; https://doi.org/10.3390/molecules24234290 - 25 Nov 2019
Cited by 6 | Viewed by 4102
Abstract
The synthetic antimicrobial peptide SET-M33 is being developed as a possible new antibacterial candidate for the treatment of multi-drug resistant bacteria. SET-M33 is a branched peptide featuring higher resistance and bioavailability than its linear analogues. SET-M33 shows antimicrobial activity against different species of [...] Read more.
The synthetic antimicrobial peptide SET-M33 is being developed as a possible new antibacterial candidate for the treatment of multi-drug resistant bacteria. SET-M33 is a branched peptide featuring higher resistance and bioavailability than its linear analogues. SET-M33 shows antimicrobial activity against different species of multi-resistant Gram-negative bacteria, including clinically isolated strains of Pseudomonas aeruginosa, Klebsiella pneumoniae, Acinetobacter baumanii and Escherichia coli. The secondary structure of this 40 amino acid peptide was investigated by NMR to fully characterize the product in the framework of preclinical studies. The possible presence of helixes or β-sheets in the structure had to be explored to predict the behavior of the branched peptide in solution, with a view to designing a formulation for parenteral administration. Since the final formulation of SET-M33 will be strictly defined in terms of counter-ions and additives, we also report the studies on a new salt form, SET-M33 chloride, that retains its activity against Gram-negative bacteria and gains in solubility, with a possible improvement in the pharmacokinetic profile. The opportunity of using a chloride counter-ion is very convenient from a process development point of view and did not increase the toxicity of the antimicrobial drug. Full article
(This article belongs to the Special Issue Peptide-Lead Drug Discovery)
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Review

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13 pages, 4743 KiB  
Review
Application of Post Solid-Phase Oxime Ligation to Fine-Tune Peptide–Protein Interactions
by Xue Zhi Zhao, Fa Liu and Terrence R. Burke, Jr.
Molecules 2020, 25(12), 2807; https://doi.org/10.3390/molecules25122807 - 18 Jun 2020
Cited by 1 | Viewed by 2781
Abstract
Protein–protein interactions (PPIs) represent an extremely attractive class of potential new targets for therapeutic intervention; however, the shallow extended character of many PPIs can render developing inhibitors against them as exceptionally difficult. Yet this problem can be made tractable by taking advantage of [...] Read more.
Protein–protein interactions (PPIs) represent an extremely attractive class of potential new targets for therapeutic intervention; however, the shallow extended character of many PPIs can render developing inhibitors against them as exceptionally difficult. Yet this problem can be made tractable by taking advantage of the fact that large interacting surfaces are often characterized by confined “hot spot” regions, where interactions contribute disproportionately to overall binding energies. Peptides afford valuable starting points for developing PPI inhibitors because of their high degrees of functional diversity and conformational adaptability. Unfortunately, contacts afforded by the 20 natural amino acids may be suboptimal and inefficient for accessing both canonical binding interactions and transient “cryptic” binding pockets. Oxime ligation represents a class of biocompatible “click” chemistry that allows the structural diversity of libraries of aldehydes to be rapidly evaluated within the context of a parent oxime-containing peptide platform. Importantly, oxime ligation represents a form of post solid-phase diversification, which provides a facile and empirical means of identifying unanticipated protein–peptide interactions that may substantially increase binding affinities and selectivity. The current review will focus on the authors’ use of peptide ligation to optimize PPI antagonists directed against several targets, including tumor susceptibility gene 101 (Tsg101), protein tyrosine phosphatases (PTPases) and the polo-like kinase 1 (Plk1). This should provide insights that can be broadly directed against an almost unlimited range of physiologically important PPIs. Full article
(This article belongs to the Special Issue Peptide-Lead Drug Discovery)
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