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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: closed (10 May 2024) | Viewed by 3607

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

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Published Papers (2 papers)

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29 pages, 3133 KiB  
Review
Comprehensive Review on Bimolecular Fluorescence Complementation and Its Application in Deciphering Protein–Protein Interactions in Cell Signaling Pathways
by Houming Ren, Qingshan Ou, Qian Pu, Yuqi Lou, Xiaolin Yang, Yujiao Han and Shiping Liu
Biomolecules 2024, 14(7), 859; https://doi.org/10.3390/biom14070859 - 17 Jul 2024
Viewed by 1706
Abstract
Signaling pathways are responsible for transmitting information between cells and regulating cell growth, differentiation, and death. Proteins in cells form complexes by interacting with each other through specific structural domains, playing a crucial role in various biological functions and cell signaling pathways. Protein–protein [...] Read more.
Signaling pathways are responsible for transmitting information between cells and regulating cell growth, differentiation, and death. Proteins in cells form complexes by interacting with each other through specific structural domains, playing a crucial role in various biological functions and cell signaling pathways. Protein–protein interactions (PPIs) within cell signaling pathways are essential for signal transmission and regulation. The spatiotemporal features of PPIs in signaling pathways are crucial for comprehending the regulatory mechanisms of signal transduction. Bimolecular fluorescence complementation (BiFC) is one kind of imaging tool for the direct visualization of PPIs in living cells and has been widely utilized to uncover novel PPIs in various organisms. BiFC demonstrates significant potential for application in various areas of biological research, drug development, disease diagnosis and treatment, and other related fields. This review systematically summarizes and analyzes the technical advancement of BiFC and its utilization in elucidating PPIs within established cell signaling pathways, including TOR, PI3K/Akt, Wnt/β-catenin, NF-κB, and MAPK. Additionally, it explores the application of this technology in revealing PPIs within the plant hormone signaling pathways of ethylene, auxin, Gibberellin, and abscisic acid. Using BiFC in conjunction with CRISPR-Cas9, live-cell imaging, and ultra-high-resolution microscopy will enhance our comprehension of PPIs in cell signaling pathways. Full article
(This article belongs to the Special Issue Advances in Protein–Protein Interactions and Reversible Self-Association)
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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://doi.org/10.3390/biom13121703 - 24 Nov 2023
Cited by 2 | Viewed by 1484
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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