Inert polymer crowders drive phase separation of polyampholyte-like proteins by enhancing electrostatic correlation
- 23 September 2026
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review E
- Vol. 114 (3) , 035430
Abstract
Inert polymer crowders ubiquitously promote the liquid-liquid phase separation (LLPS) of intrinsically disordered proteins (IDPs), yet the underlying mechanisms remain elusive. By evaluating the potential of mean force between polyampholyte-like IDPs, we demonstrate that the presence of inert polymer crowders induces conformational transitions by screening the excluded-volume interactions of the IDPs, indirectly enhancing interchain electrostatic correlations. Under physiological conditions, this enhanced correlation is sufficient to trigger LLPS of highly charged IDPs that would otherwise remain dispersed. Our work highlights a universal crowder-conformation-electrostatics coupling in driving LLPS.Keywords
Funding Information
- National Natural Science Foundation of China
This publication has 58 references indexed in Scilit:
- LAMMPS - a flexible simulation tool for particle-based materials modeling at the atomic, meso, and continuum scalesComputer Physics Communications, 2022
- G3BP1 Is a Tunable Switch that Triggers Phase Separation to Assemble Stress GranulesCell, 2020
- A Molecular Grammar Governing the Driving Forces for Phase Separation of Prion-like RNA Binding ProteinsCell, 2018
- Phase Separation of FUS Is Suppressed by Its Nuclear Import Receptor and Arginine MethylationCell, 2018
- Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule AssemblyCell Reports, 2018
- TIA-1 Self-Multimerization, Phase Separation, and Recruitment into Stress Granules Are Dynamically Regulated by Zn2+Cell Reports, 2018
- Compositional Control of Phase-Separated Cellular BodiesCell, 2016
- Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological FibrillizationCell, 2015
- A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease MutationCell, 2015
- Interaction between particles suspended in solutions of macromoleculesJournal of Polymer Science, 1958