Protein Interactions at the Molecular Scale: From Mechanisms to Applications

A special issue of Biophysica (ISSN 2673-4125).

Deadline for manuscript submissions: 31 July 2026 | Viewed by 1193

Special Issue Editor


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Guest Editor
Department of Physics and Astronomy, Rutgers University, Piscataway, NJ, USA
Interests: proteins; evolution; structure; function

Special Issue Information

Dear Colleagues,

The importance of hydrophobic interactions in proteins is well known; it goes well beyond protein folding and often dominates evolutionary trends in protein functions. Although the most hydrophobic amino acids are known, the collective effects of hydrophobic interactions on protein binding are seldom quantified, even in molecular dynamics simulations.

The aim of this Special Issue is to collate and present experimental and/or theoretical studies of protein–molecule binding that explore the role of protein hydrophobic regions and alternative critical regions.

Dr. James C. Phillips
Guest Editor

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Keywords

  • hydrophobicity
  • amino acid
  • length scale
  • interface
  • transition

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Published Papers (1 paper)

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Review

35 pages, 1499 KB  
Review
The Pharmacology and Dual Role of Proteostasis in Amyloidoses
by Angela Albanese, Manasi M. Natu and Paul M. Seidler
Biophysica 2026, 6(2), 31; https://doi.org/10.3390/biophysica6020031 - 12 Apr 2026
Viewed by 678
Abstract
Cellular protein quality control comprises the ubiquitin proteasome system, autophagy, and molecular chaperones, which maintain proteostasis in healthy tissues. The failure of these cellular and molecular pathways, which normally safeguard the proteome, can cause and even exacerbate amyloidoses, the abnormal accumulation of proteins [...] Read more.
Cellular protein quality control comprises the ubiquitin proteasome system, autophagy, and molecular chaperones, which maintain proteostasis in healthy tissues. The failure of these cellular and molecular pathways, which normally safeguard the proteome, can cause and even exacerbate amyloidoses, the abnormal accumulation of proteins into amyloid fibrils that drive neurodegeneration. Amyloidoses can also damage peripheral organs; examples include light chain amyloidosis, cardiac amyloidosis, and renal amyloidosis. Restoring proteostasis and preventing protein aggregation is therefore an active area of research, with several promising strategies under investigation. Among these approaches, small-molecule modulators that restore proteostasis are attractive candidates because they may simultaneously rescue multiple quality control mechanisms and remodel aggregates to improve their accessibility to endogenous degradation pathways. Here, we propose that amyloid pathology disrupts multiple proteostasis pathways simultaneously, creating a feedforward cascade in which the breakdown of interconnected proteostasis networks drives progressive protein aggregation, which in turn propels proteostasis collapse. Pharmacological interventions targeting protein aggregation offer opportunity to rescue interconnected proteostasis networks, which could, in turn, cooperatively manage or eliminate pathogenic amyloid burden. Full article
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