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Editorial Board Members’ Collection Series: “Protein Biophysics”

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biophysics".

Deadline for manuscript submissions: 31 October 2024 | Viewed by 816

Special Issue Editors


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Guest Editor
Department of Molecular Medicine, University of South Florida, Tampa, FL, USA
Interests: protein folding; protein misfolding; intrinsically disordered proteins
Special Issues, Collections and Topics in MDPI journals

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Guest Editor
Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel
Interests: peptides; peptide chemistry; protein interactions; medicinal chemistry; intrinsically disordered proteins

Special Issue Information

Dear Colleagues,

The Editorial Board Members’ Collection Series: “Protein Biophysics” aims to collect high-quality research articles, short communications, and review articles in all the fields of protein biophysics. We encourage Editorial Board Members of the Molecular Biophysics Section of the International Journal of Molecular Sciences to contribute papers reflecting the latest progress in their research field.

Topics include, but are not limited to, the following:

  • Protein Structure and Prediction;
  • Protein Biophysics;
  • Protein Dynamics;
  • Peptide and Protein Aggregation;
  • Protein Misfolding;
  • Protein Folding;
  • Protein Stability;
  • Protein Function;
  • Posttranslational Modifications;
  • Intrinsically Disordered Proteins;
  • Protein–Ligand Interactions;
  • Protein–Protein Interactions;
  • Protein–Nucleic Acid Interactions;
  • Membrane Proteins;
  • Liquid–Liquid Phase Separation.

Prof. Dr. Vladimir N. Uversky
Prof. Dr. Assaf Friedler
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 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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • protein structure and prediction
  • protein biophysics
  • protein dynamics
  • peptide and protein aggregation
  • protein misfolding
  • protein folding
  • protein stability
  • protein function
  • posttranslational modifications
  • intrinsically disordered proteins
  • protein–ligand interactions
  • protein–protein interactions
  • protein–nucleic acid interactions
  • membrane proteins
  • liquid–liquid phase separation

Published Papers (1 paper)

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Research

16 pages, 2600 KiB  
Article
The Development of CDC25A-Derived Phosphoseryl Peptides That Bind 14-3-3ε with High Affinities
by Seraphine Kamayirese, Sibaprasad Maity, Laura A. Hansen and Sándor Lovas
Int. J. Mol. Sci. 2024, 25(9), 4918; https://doi.org/10.3390/ijms25094918 - 30 Apr 2024
Viewed by 493
Abstract
Overexpression of the 14-3-3ε protein is associated with suppression of apoptosis in cutaneous squamous cell carcinoma (cSCC). This antiapoptotic activity of 14-3-3ε is dependent on its binding to CDC25A; thus, inhibiting 14-3-3ε – CDC25A interaction is an attractive therapeutic approach to promote apoptosis [...] Read more.
Overexpression of the 14-3-3ε protein is associated with suppression of apoptosis in cutaneous squamous cell carcinoma (cSCC). This antiapoptotic activity of 14-3-3ε is dependent on its binding to CDC25A; thus, inhibiting 14-3-3ε – CDC25A interaction is an attractive therapeutic approach to promote apoptosis in cSCC. In this regard, designing peptide inhibitors of 14-3-3ε – CDC25A interactions is of great interest. This work reports the rational design of peptide analogs of pS, a CDC25A-derived peptide that has been shown to inhibit 14-3-3ε–CDC25A interaction and promote apoptosis in cSCC with micromolar IC50. We designed new peptide analogs in silico by shortening the parent pS peptide from 14 to 9 amino acid residues; then, based on binding motifs of 14-3-3 proteins, we introduced modifications in the pS(174–182) peptide. We studied the binding of the peptides using conventional molecular dynamics (MD) and steered MD simulations, as well as biophysical methods. Our results showed that shortening the pS peptide from 14 to 9 amino acids reduced the affinity of the peptide. However, substituting Gln176 with either Phe or Tyr amino acids rescued the binding of the peptide. The optimized peptides obtained in this work can be candidates for inhibition of 14-3-3ε – CDC25A interactions in cSCC. Full article
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