This exposition reveals the effect of glucose as a molecular crowder on the solvent environment in proximity of the protein surface in putative folded (Ubiquitin) and intrinsically disordered (dimeric Amyloid beta) states. Atomistic simulations reveal markedly higher structural perturbation in the disordered systems due to crowding effects, while the folded state retains overall structural fidelity. Key hydrophobic contacts in the disordered dimer are lost. However, glucose induced crowding results in elevated hydration on surfaces of both protein systems. Despite evident differences in their structural responses, the hydration layer of both the folded and disordered states display a distinct enhancement in lifetimes of mean residence and rotational relaxation under the hyperglycemic conditions. The results are crucial in the light of emergent co-solvent induced biological phenomena in crowded media.

该阐述揭示了葡萄糖作为分子聚集物对蛋白质表面附近的溶剂环境的影响，假定折叠（泛素）和本质无序（二聚淀粉样蛋白）状态。原子模拟显示，由于拥挤效应，无序系统中的结构扰动明显更高，而折叠状态保持整体结构保真度。无序二聚体中的关键疏水接触丢失。然而，葡萄糖诱导的拥挤会导致两种蛋白质系统表面的水合作用增加。尽管它们的结构响应存在明显差异，但折叠和无序状态的水合层在高血糖条件下显示出平均停留和旋转松弛寿命的明显增强。