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Special Issue "Advances in Research of Short Peptides"

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

Deadline for manuscript submissions: 31 December 2020.

Special Issue Editors

Dr. Joanna Bojarska
Website
Guest Editor
Lodz University of Technology, Faculty of Chemistry, Lodz, Poland
Interests: bio-supramolecular chemistry of oligopeptides; polymorphism; biologically active substances; drug design
Prof. Dr. Wojciech M. Wolf
Website
Guest Editor
Lodz University of Technology, Faculty of Chemistry, Lodz, Poland
Interests: X-ray crystallography; supramolecular chemistry; crystal engineering; peptides; medicinal chemistry; coordination chemistry; solid-state synthesis; analytical chemistry
Prof. Dr. Milan Remko
Website
Co-Guest Editor
Remedika, Bratislava, Slovakia
Interests: theoretical chemistry; research of drugs; drug-receptor interactions; structure of intermolecular complexes; peptides
Prof. Dr. Piotr Zielenkiewicz
Website
Co-Guest Editor
Polish Academy of Sciences, Institute of Biochemistry and Biophysics, Warsaw, Poland
Interests: bioinformatics; theoretical molecular biophysics; biochemistry of proteins
Prof. Dr. Michele Saviano
Website
Co-Guest Editor
Istituto di Cristallografia, Consiglio Nazionale delle Ricerche, Bari, Italy
Interests: biocrystallography, drug design; peptide chemistry
Prof. Dr. Janusz Zabrocki
Website
Co-Guest Editor
Institute of Organic Chemistry, Lodz University of Technology, Faculty of Chemistry, Lodz, Poland
Interests: peptide chemistry; synthesis of medicinal compounds; peptidomimetics; neuropeptides
Dr. Krzysztof Kaczmarek
Website
Co-Guest Editor
Institute of Organic Chemistry, Lodz University of Technology, Faculty of Chemistry, Lodz, Poland
Interests: peptide chemistry; peptide synthesis; unusual amino acids; peptide bond motifs

Special Issue Information

Dear Colleagues,

It is a great honor for us to invite you to a Special Issue of “Molecules” focusing on short peptides, which have attracted increasing interest due to their many advantages and applications, inter alia anticancer therapies or hydrogels. They represent an unique class of biopharmaceuticals, including cosmeceuticals, with improved pharmacological profiles. Oligopeptides fill the gap between classical small molecules and mature proteins. Amino acids carry the prime structural information and are building blocks of higher level species, which architecture is mainly controlled by intermolecular interactions, which just like a virtuoso play a symphony of life. Therefore, detailed knowledge on interactions either at a molecular or supramolecular level is essential in the development of innovative medical therapies or smart functional biomaterials. Notably, small molecules and proteins have a natural synergy. The Cambridge Structure Database (CSD) collects over one million crystal structures of small molecules and is the world`s largest source of precise information geometry of either bonding or non-bonding interactions. The latter may be systematized into the libraries of supramolecular synthons, which can be further transferred to the macromolecular environment. The CSD data may be used for screening of ligand-target binding affinities. New computational methods for characterizing molecular shapes, electrostatic complementarity and the intercontacts surfaces as related to their environment, like Hirshfeld surface analysis, can be effective tools in the drug discovery. The combination of information from the CSD and the RCSB Protein Data Bank yield thorough foundation for the smart structure and ligand based design.

We cordially invite scientists from various fields to submit research articles, reviews or communications concerning molecular and supramolecular aspects of short peptides and modified amino acids investigated by either experimental or/and in silico methods. Findings leading to novel therapeutics and functional materials are particularly welcome.

Dr. Joanna Bojarska
Prof. Dr. Wojciech M. Wolf
Prof. Dr. Milan Remko
Prof. Dr. Piotr Zielenkiewicz
Prof. Dr. Michele Saviano
Prof. Dr. Janusz Zabrocki
Dr. Krzysztof Kaczmarek
Prof. Dr. Michele Saviano
Guest Editors

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 papers will be 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 2000 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

  • oligopeptide-based therapeutic agents and functional biomaterials
  • molecular and supramolecular features
  • drug design
  • drug-receptor interactions
  • synthesis of oligopeptides and modified amino acids

Published Papers (3 papers)

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Research

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Open AccessArticle
The Reactions of H2O2 and GSNO with the Zinc Finger Motif of XPA. Not A Regulatory Mechanism, But No Synergy with Cadmium Toxicity
Molecules 2020, 25(18), 4177; https://doi.org/10.3390/molecules25184177 - 12 Sep 2020
Abstract
Tetrathiolate zinc fingers are potential targets of oxidative assault under cellular stress conditions. We used the synthetic 37-residue peptide representing the tetrathiolate zinc finger domain of the DNA repair protein XPA, acetyl-DYVICEECGKEFMSYLMNHFDLPTCDNCRDADDKHK-amide (XPAzf) as a working model to study the reaction of its [...] Read more.
Tetrathiolate zinc fingers are potential targets of oxidative assault under cellular stress conditions. We used the synthetic 37-residue peptide representing the tetrathiolate zinc finger domain of the DNA repair protein XPA, acetyl-DYVICEECGKEFMSYLMNHFDLPTCDNCRDADDKHK-amide (XPAzf) as a working model to study the reaction of its Zn(II) complex (ZnXPAzf) with hydrogen peroxide and S-nitrosoglutathione (GSNO), as oxidative and nitrosative stress agents, respectively. We also used the Cd(II) substituted XPAzf (CdXPAzf) to assess the situation of cadmium assault, which is accompanied by oxidative stress. Using electrospray mass spectrometry (ESI-MS), HPLC, and UV-vis and circular dichroism spectroscopies we demonstrated that even very low levels of H2O2 and GSNO invariably cause irreversible thiol oxidation and concomitant Zn(II) release from ZnXPAzf. In contrast, CdXPAzf was more resistant to oxidation, demonstrating the absence of synergy between cadmium and oxidative stresses. Our results indicate that GSNO cannot act as a reversible modifier of XPA, and rather has a deleterious effect on DNA repair. Full article
(This article belongs to the Special Issue Advances in Research of Short Peptides)
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Open AccessArticle
Antinociceptive and Cytotoxic Activity of Opioid Peptides with Hydrazone and Hydrazide Moieties at the C-Terminus
Molecules 2020, 25(15), 3429; https://doi.org/10.3390/molecules25153429 - 28 Jul 2020
Abstract
In the present contribution, we analyze the influence that C-terminal extension of short opioid peptide sequences by organic fragments has on receptor affinity, in vivo analgesic activity, and antimelanoma properties. The considered fragments were based on either N-acylhydrazone (NAH) or N′-acylhydrazide [...] Read more.
In the present contribution, we analyze the influence that C-terminal extension of short opioid peptide sequences by organic fragments has on receptor affinity, in vivo analgesic activity, and antimelanoma properties. The considered fragments were based on either N-acylhydrazone (NAH) or N′-acylhydrazide motifs combined with the 3,5-bis(trifluoromethyl)phenyl moiety. Eleven novel compounds were synthesized and subject to biological evaluation. The analyzed compounds exhibit a diversified range of affinities for the µ opioid receptor (MOR), rather low δ opioid receptor (DOR) affinities, and no appreciable neurokinin-1 receptor binding. In three out of four pairs, N-acylhydrazone-based derivatives bind MOR better than their N’-acylhydrazide counterparts. The best of the novel derivatives have similar low nanomolar MOR binding affinity as the reference opioids, such as morphine and biphalin. The obtained order of MOR affinities was compared to the results of molecular docking. In vivo, four tested compounds turned out to be relatively strong analgesics. Finally, the NAH-based analogues reduce the number of melanoma cells in cell culture, while their N′-acylhydrazide counterparts do not. The antimelanoma properties are roughly correlated to the lipophilicity of the compounds. Full article
(This article belongs to the Special Issue Advances in Research of Short Peptides)
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Review

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Open AccessReview
Peptides with Dual Antimicrobial–Anticancer Activity: Strategies to Overcome Peptide Limitations and Rational Design of Anticancer Peptides
Molecules 2020, 25(18), 4245; https://doi.org/10.3390/molecules25184245 - 16 Sep 2020
Abstract
Peptides are naturally produced by all organisms and exhibit a wide range of physiological, immunomodulatory, and wound healing functions. Furthermore, they can provide with protection against microorganisms and tumor cells. Their multifaceted performance, high selectivity, and reduced toxicity have positioned them as effective [...] Read more.
Peptides are naturally produced by all organisms and exhibit a wide range of physiological, immunomodulatory, and wound healing functions. Furthermore, they can provide with protection against microorganisms and tumor cells. Their multifaceted performance, high selectivity, and reduced toxicity have positioned them as effective therapeutic agents, representing a positive economic impact for pharmaceutical companies. Currently, efforts have been made to invest in the development of new peptides with antimicrobial and anticancer properties, but the poor stability of these molecules in physiological environments has triggered a bottleneck. Therefore, some tools, such as nanotechnology and in silico approaches can be applied as alternatives to try to overcome these obstacles. In silico studies provide a priori knowledge that can lead to the development of new anticancer peptides with enhanced biological activity and improved stability. This review focuses on the current status of research in peptides with dual antimicrobial–anticancer activity, including advances in computational biology using in silico analyses as a powerful tool for the study and rational design of these types of peptides. Full article
(This article belongs to the Special Issue Advances in Research of Short Peptides)
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