纳米生物界面对淀粉样蛋白聚集的调控机制研究

Regulation mechanism of nanobiointerfaces in amyloid peptide assembly and aggregation structures

本文以阿尔兹海默症的致病多肽β淀粉样蛋白(Aβ)为例,介绍了疾病相关淀粉样蛋白的分子精细结构、组装和聚集过程、聚集体形貌及神经细胞毒性的研究进展,并在此基础上以纳米生物界面对于淀粉样蛋白构象、组装结构、聚集动力学、神经细胞毒性等生物功能的调控机制进行研究.从分子水平上分析和探讨了纳米生物界面与淀粉样蛋白分子或者聚集体的相互作用方式和机理,有助于加深对淀粉样多肽和调节剂之间复杂多样的相互作用方式的理解,对深入了解淀粉样多肽的组装机理和调控机制以及探索治疗神经退行性疾病的药物设计等方面具有较大意义.

In this review, we try to reflect the recent progress on assembly structures, aggregation behaviors and the cytotoxicity of beta amyloid(Aβ) peptides, which are closely related to the pathogenesis of Alzheimer’s disease(AD).Based on these studies, the progress on the regulation mechanism of various nanobiointerfaces in amyloid peptide assembly and aggregation structures is reviewed and discussed, especially the interaction patterns and mechanisms between Aβ peptides and nanomaterials on the molecule level. These progresses could help to deepen the insights of the complex interactions between amyloid peptides and modulators. To study Aβ peptide conformation, assembly mechanism and aggregation process, developing new efficient nanobiointerface modulators is of great importance for the therapeutic strategy evolution.