Lee Chiu Fan
Physics Department, Clarendon Laboratory, Oxford University, Parks Road, Oxford OX1 3PU, United Kingdom.
Phys Rev E Stat Nonlin Soft Matter Phys. 2009 Sep;80(3 Pt 1):031922. doi: 10.1103/PhysRevE.80.031922. Epub 2009 Sep 30.
Protein aggregation in the form of amyloid fibrils has important biological and technological implications. Although the self-assembly process is highly efficient, aggregates not in the fibrillar form would also occur and it is important to include these disordered species when discussing the thermodynamic equilibrium behavior of the system. Here, we initiate such a task by considering a mixture of monomeric proteins and the corresponding aggregates in the disordered form (micelles) and in the fibrillar form (amyloid fibrils). Starting with a model on the respective binding free energies for these species, we calculate their concentrations at thermal equilibrium. We then discuss how the incorporation of the disordered structure furthers our understanding on the various amyloid promoting factors observed empirically, and on the kinetics of fibrilization.
淀粉样原纤维形式的蛋白质聚集具有重要的生物学和技术意义。尽管自组装过程效率很高，但也会出现非纤维状的聚集体，在讨论系统的热力学平衡行为时，纳入这些无序物种很重要。在此，我们通过考虑单体蛋白与无序形式（胶束）和纤维状形式（淀粉样原纤维）的相应聚集体的混合物来启动这项任务。从这些物种各自结合自由能的模型出发，我们计算它们在热平衡时的浓度。然后，我们讨论无序结构的纳入如何进一步加深我们对凭经验观察到的各种淀粉样蛋白促进因子以及纤维化动力学的理解。
