Fernández Ariel, de las Mercedes Boland Maria
Institute for Biophysical Dynamics, The University of Chicago, Chicago, IL 60637, USA.
FEBS Lett. 2002 Oct 9;529(2-3):298-301. doi: 10.1016/s0014-5793(02)03392-6.
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.
在涉及蛋白质折叠和聚集的竞争情况下，阐明了分子拥挤诱导的溶剂结构效应。选择淀粉样蛋白生成蛋白的两个模式片段作为研究案例，并通过对溶剂进行隐式处理的分子动力学进行分析。确定了诱导聚集所需的拥挤程度。这些结果是评估体内环境在理解纤维形成中的相关性的第一步。通过令人满意地重现全原子显式溶剂轨迹的结果，独立验证了该方法。
