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ORIGINAL RESEARCH article

Front. Nanotechnol.
Sec. Nanophotonics
Volume 7 - 2025 | doi: 10.3389/fnano.2025.1556384
This article is part of the Research Topic Emerging Leaders in Nanotechnology View all 4 articles

Protein Modifications and Ionic Strength Show the Difference Between Protein-Mediated and Solvent-mediated Regulation of Biomolecular Condensation

Provisionally accepted
Ellen Adams Ellen Adams 1,2*Artur Czajkowski Artur Czajkowski 1,2Abhirami Udayabanu Abhirami Udayabanu 1,2Manthan Raj Manthan Raj 1,2Likhitha P Ch Likhitha P Ch 1,2Marija Tursunović Marija Tursunović 3Marcus Jahnel Marcus Jahnel 1
  • 1 Technical University Dresden, Dresden, Germany
  • 2 Institute of Resource Ecology, Helmholtz Center Dresden-Rossendorf, Helmholtz Association of German Research Centers (HZ), Dresden, Lower Saxony, Germany
  • 3 University of Belgrade, Belgrade, Serbia

The final, formatted version of the article will be published soon.

    Biomolecular condensation is an important mechanism of cellular compartmentalization without membranes. Formation of liquid-like condensates of biomolecules involves protein-protein interactions working in tandem with protein-water interactions. The balance of these interactions in condensate-forming proteins is impacted by multiple factors inside of a living organism. This work investigates the effects of post-translational modifications (PTMs) and salt concentration as two such perturbing factors on the protein Fused in Sarcoma (FUS), an RNA binding protein. Attenuated total reflection Terahertz spectroscopy is used to probe the solvation behavior in condensates formed from FUS protein with and without PTMs at 100 mM and 2.5 M KCl. The results show that while PTMs impact the phase-separating propensity, they do not alter protein solvation in the condensate. On the other hand, salt concentration was found to alter the stiffness of the water hydrogen bond network. These findings have implications for biomolecular condensates chemistry, showing that condensate molecular organization is perturbed by fluctutations in solvent properties.

    Keywords: biomolecular condensates, Protein solvation, THz Spectroscopy, reentrant phase separation, post-translational modifications

    Received: 06 Jan 2025; Accepted: 05 Feb 2025.

    Copyright: © 2025 Adams, Czajkowski, Udayabanu, Raj, Ch, Tursunović and Jahnel. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence: Ellen Adams, Technical University Dresden, Dresden, Germany

    Disclaimer: All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.