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Peptides as Candidate Chemotherapeutic Drugs

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

Deadline for manuscript submissions: closed (10 May 2016) | Viewed by 5868

Special Issue Editor


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Guest Editor
Department of Pharmaceutics and Medicinal Chemistry, University of Pacific, 3601 Pacific Ave, Stockton, CA 95211, USA
Interests: drug design; synthesis; peptides; peptidomimetics; kinase inhibitors; cancer

Special Issue Information

Dear Colleagues,

Peptides, whether derived from natural or non-natural amino acids, hold enormous potential as drug molecules due to their ability to serve as surrogate substrates or interaction partners of proteins that are relevant drug targets. While there are many peptide drugs approved for clinical use, this chemical class still lags, in number, behind small molecules and therapeutic proteins (including antibodies). Peptides suffer from the stigma of displaying generally poor pharmacokinetic properties, including poor bioavailability, absorption, and short in vivo
half-life, and the potential for expensive large scale production. In the last several decades, strategies and techniques have been developed to deal with these concerns. In recent years there has been resurgent interest in peptides as drug molecules. This Special Issue of Molecules aims to present advances in addressing unique difficulties in development of peptides as drugs for the traditional chemotherapy areas of anti-infective agents and cancer. We welcome submission of original research papers, as well as reviews for this issue.

Dr. Wade A. Russu
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

  • peptides
  • peptide synthesis
  • chemotherapy
  • anti-infective
  • anticancer
  • drug development
  • drug targeting

Published Papers (1 paper)

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Research

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Article
Influence of Cysteine and Tryptophan Substitution on DNA-Binding Activity on Maize α-Hairpinin Antimicrobial Peptide
by Daniel A. Sousa, William F. Porto, Maria Z. Silva, Tatiane R. Da Silva and Octávio L. Franco
Molecules 2016, 21(8), 1062; https://doi.org/10.3390/molecules21081062 - 13 Aug 2016
Cited by 29 | Viewed by 5634
Abstract
For almost four decades, antimicrobial peptides have been studied, and new classes are being discovered. However, for therapeutic use of these molecules, issues related to the mechanism of action must be answered. In this work, the antimicrobial activity of the hairpinin MBP-1 was [...] Read more.
For almost four decades, antimicrobial peptides have been studied, and new classes are being discovered. However, for therapeutic use of these molecules, issues related to the mechanism of action must be answered. In this work, the antimicrobial activity of the hairpinin MBP-1 was studied by the synthesis of two variants, one replacing cysteines and one tryptophan with alanine. Antibacterial activity was abolished in both variants. No membrane disturbance, even in concentrations higher than those required to inhibit the bacteria, was observed in SEM microscopy. The gel retardation assay showed that MBP-1 possesses a higher DNA-binding ability than variants. Finally, molecular modelling showed that the lack of cysteines resulted in structure destabilization and lack of tryptophan resulted in a less flexible peptide, with less solvent assessable surface area, both characteristics that could contribute to absence of activity. In summary, the data here reported add more information about the multiple mechanisms of action of α-hairpinins. Full article
(This article belongs to the Special Issue Peptides as Candidate Chemotherapeutic Drugs)
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