Solvent environment conducive to protein aggregation.

The effect of solvent structuring induced by molecular crowding is elucidated within a competitive situation involving protein folding and aggregation. Two patterned fragments of amyloidogenic proteins are chosen as study cases and analyzed by molecular dynamics with an implicit treatment of the solvent. The extent of crowding needed to induce aggregation is determined. The results constitute a first step to assess the relevance of in vivo environments in understanding fibrillogenesis. The approach is independently validated by satisfactorily reproducing the results of an all-atom explicit solvent trajectory.