Matubayasi, Nobuyuki and Do, Tuan Minh and Horinek, Dominik (2025) Free-energy analysis of cosolvent effects on biomolecular aggregation. POLYMER JOURNAL, 57 (8). pp. 773-784. ISSN 0032-3896, 1349-0540
Full text not available from this repository. (Request a copy)Abstract
A theoretical-computational scheme for analyzing the effect of an added cosolvent on the aggregation equilibrium of a biomolecule is presented. The scheme is based on the relation that the derivative of the excess chemical potential with respect to the cosolvent concentration is determined by the corresponding derivative of the solvation free energy averaged over the solute configurations. The role of solvation is highlighted in the cosolvent-induced shift in the aggregation equilibrium of a biomolecule, and an illustrative analysis with all-atom models is provided for an amyloid peptide by employing the energy-representation method to compute the solvation free energy. Adenosine triphosphate (ATP) and urea are adopted as a cosolvent added to water, and the former is seen to inhibit aggregation more effectively than the latter. The solvation free energy is decomposed into the contributions from intermolecular-interaction components such as electrostatic, van der Waals, and excluded-volume, and it is found that the cosolvent effects are governed by the van der Waals interaction for both of ATP and urea.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SOLVATION FREE-ENERGIES; REPRESENTATION; MOLECULES; ATP; THERMODYNAMICS; A-BETA(16-22); SIMULATION; BINDING |
| Subjects: | 500 Science > 540 Chemistry & allied sciences |
| Divisions: | Chemistry and Pharmacy > Institut für Physikalische und Theoretische Chemie > Chair of Chemistry VI - Physical Chemistry (Solution Chemistry) > Prof. Dr. Dominik Horinek |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 15 Jul 2026 09:29 |
| Last Modified: | 15 Jul 2026 09:29 |
| URI: | https://pred.uni-regensburg.de/id/eprint/66820 |
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