A theoretical-computational scheme is formulated to analyze the shift in the aggregation equilibrium of a biomolecule upon addition of a cosolvent. The cosolvent-induced change in the solvation free energy plays the central role in the formulation, and it is shown for a model peptide that the ATP and urea cosolvents make the solvent environment more favorable for dissociated monomers than for aggregates. The effect of ATP to inhibit aggregation is brought by van der Waals interactions due to cancellation of the electrostatic effects between ATP and water.
- Nobuyuki Matubayasi
- Tuan Minh Do
- Dominik Horinek
