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Biomolecules
Special Issues
Advances in Protein–Protein Interactions and Reversible Self-Association
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Advances in Protein–Protein Interactions and Reversible Self-Association

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Biomacromolecules: Proteins".

Deadline for manuscript submissions: 10 May 2024 | Viewed by 1144

Special Issue Editors

Dr. Robin Curtis

E-Mail Website
Guest Editor
Manchester Institute of Biotechnology, Department of Chemical Engineering, Faculty of Science and Engineering, The University of Manchester, Manchester M1 7DN, UK
Interests: protein aggregation; phase separation; protein-protein and protein-solvent interactions; biopharmaceuticals; light scattering
Prof. Dr. Christopher J. Roberts

E-Mail Website
Guest Editor
Chemical and Biomolecular Engineering, University of Delaware, Newark, DE 19716, USA
Interests: protein aggregation and stability; protein phase behavior; protein-protein interactions

Special Issue Information

Dear Colleagues,

Crucial for research and development of protein therapeutics or biopharmaceuticals is knowledge of protein-protein interactions (PPIs) and protein reversible self association.  These dictate protein self-assembly patterns and solution properties, which must be controlled for cost-effective manufacturing. In recent years, there has been much progress and advances made towards our molecular understanding of protein-protein interactions that has paralleled the rapid growth in the antibody therapeutics market.

This issue invites articles covering the most recent experimental and computational developments in characterizing the structural determinants and molecular basis for protein-protein and protein-cosolvent (co-solute) interactions, and the relationship to protein phase behaviour (crystallization, liquid-liquid phase separation, opalescence, and gelation), concentrated solution rheological properties, and protein misfolding and aggregation. Aggregation, in particular, has remained a significant and challenging problem to solve due to difficulties in characterizing partially folded intermediates and their colloidal stabilities.  We expect some of the recent advances will shed novel insights into mechanisms and transient protein interactions controlling the stability, and dynamics of biological condensates, which are formed through processes such as liquid-liquid phase separation and are key determinants for cellular diseased states.

Dr. Robin Curtis
Prof. Dr. Christopher J. Roberts
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. Biomolecules is an international peer-reviewed open access monthly 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

  • biopharmaceuticals
  • antibodies
  • excipients
  • liquid-liquid phase separation
  • viscosity
  • reversible self association
  • protein aggregation

Published Papers (1 paper)

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Review

20 pages, 5967 KiB  
Review
Protein Association in Solution: Statistical Mechanical Modeling
by Vojko Vlachy, Yurij V. Kalyuzhnyi, Barbara Hribar-Lee and Ken A. Dill
Biomolecules 2023, 13(12), 1703; https://0-doi-org.brum.beds.ac.uk/10.3390/biom13121703 - 24 Nov 2023
Viewed by 903
Abstract
Protein molecules associate in solution, often in clusters beyond pairwise, leading to liquid phase separations and high viscosities. It is often impractical to study these multi-protein systems by atomistic computer simulations, particularly in multi-component solvents. Instead, their forces and states can be studied [...] Read more.
Protein molecules associate in solution, often in clusters beyond pairwise, leading to liquid phase separations and high viscosities. It is often impractical to study these multi-protein systems by atomistic computer simulations, particularly in multi-component solvents. Instead, their forces and states can be studied by liquid state statistical mechanics. However, past such approaches, such as the Derjaguin-Landau-Verwey-Overbeek (DLVO) theory, were limited to modeling proteins as spheres, and contained no microscopic structure–property relations. Recently, this limitation has been partly overcome by bringing the powerful Wertheim theory of associating molecules to bear on protein association equilibria. Here, we review these developments. Full article
(This article belongs to the Special Issue Advances in Protein–Protein Interactions and Reversible Self-Association)
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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Title: Phase behaviour of an integral membrane protein; Identification of a nucleation zone for OmpG
Authors: Jennifer McManus
Affiliation: University of Bristold, Bristol, United Kingdom
Abstract: To be determined

Title: To be determined
Authors: Wolfgang Frieß; et al.
Affiliation: Department of Pharmacy, University of Munich, Germany
Abstract: To be determined

Title: To be determined
Authors: Joseph E. Curtis; et al.
Affiliation: NIST Center for Neutron Research, National Institute of Standards and Technology, 100 Bureau Drive, Mail Stop 6102, Gaithersburg, MD 20899, USA
Abstract: To be determined

Title: To be determined
Authors: Keith Johnston; et al.
Affiliation: Department of Chemical Engineering, Univ. of Texas, Austin, TX, USA
Abstract: To be determined

Title: To be determined
Authors: Peter M. Tessier; et al.
Affiliation: Chemical Engineering, Pharmaceutical Sciences, B10-A179 NCRC, 2800 Plymouth Road, Ann Arbor, MI 48109-2800, USA
Abstract: To be determined

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