Protein amyloid aggregate:Structure and function  

作　　者：Qianhui Xu Yeyang Ma Yunpeng Sun Dan Li Xin Zhang Cong Liu 

机构地区：[1]Interdisciplinary Research Center on Biology and Chemistry,Shanghai Institute of Organic Chemistry,Chinese Academy of Sciences,Shanghai,China [2]Bio-X Institutes,Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders,Ministry of Education,Shanghai Jiao Tong University,Shanghai,China [3]Zhangjiang Institute for Advanced Study,Shanghai Jiao Tong University,Shanghai,China [4]Department of Chemistry and Westlake Laboratory of Life Sciences and Biomedicine,Westlake University,Hangzhou,China [5]State Key Laboratory of Bio-Organic and Natural Products Chemistry,Shanghai Institute of Organic Chemistry,University of Chinese Academy of Sciences,Shanghai,China

出　　处：《Aggregate》2023年第4期55-70,共16页聚集体（英文）

基　　金：National Natural Science Foundation(NSF)of China,Grant/Award Numbers:82188101,32171236,31872716,32170683;the Science and Technology Commission of Shanghai Municipality(STCSM),Grant/Award Numbers:20XD1425000,2019SHZDZX02;the Shanghai Pilot Program for Basic Research–Chinese Academy of Science,Shanghai Branch,Grant/Award Number:CYJ-SHFY-2022-005。

摘　　要：Protein amyloid aggregation has been widely observed to occur and plays impor-tant roles in both physiological processes and pathological diseases.Remarkably,amyloid aggregates assembled by native proteins gain a variety of different biolog-ical activities,which cannot be adopted by the unassembled protein alone.Thus,it is important to investigate the molecular basis of self-assembly of protein amyloid aggregates and how the aggregated protein structure determines its function.In the review,wefirstly introduce our structural knowledge on how different amyloid pro-teins undergo conformational transition and assemble into amyloid aggregate,with the main focus on amyloidfibril,which is the major species of amyloid aggregate.Then,we elaborate how different structures of amyloidfibrils enable them to fulfill highly diverse functions in either physiological or pathological condition.Further-more,we discuss the structural polymorph which is a very unique feature of amyloidfibril,and its implication in understanding the structure-function relationship of amy-loidfibrils.Finally,we point out the importance of applying and integrating new approaches for deepening the structure-function study of amyloidfibrils and high-light the potential of designing amyloidfibril-based functional bio-nanomaterials for application.

关 键 词：amyloidfibril neurodegenerative diseases prion-like propagation protein phase separation protein aggregate 

分 类 号：R741[医药卫生—神经病学与精神病学]