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Hierarchical processes in β-sheet peptide self-assembly from the microscopic to the mesoscopic level
引用本文:邓礼,徐海.Hierarchical processes in β-sheet peptide self-assembly from the microscopic to the mesoscopic level[J].中国物理 B,2016,25(1):18701-018701.
作者姓名:邓礼  徐海
作者单位:Centre for Bioengineering and Biotechnology, China University of Petroleum (East China), Qingdao 266580, China
基金项目:Project supported by the National Natural Science Foundation of China (Grant Nos. 21373270 and 11504431) and the Fundamental Research Funds for Central Universities of China (Grant No. 15CX02025A).
摘    要:Under appropriate physicochemical conditions, short peptide fragments and their synthetic mimics have been shown to form elongated cross-β nanostructures through self-assembly. The self-assembly process and the resultant peptide nanostructures are not only related to neurodegenerative diseases but also provide inspiration for the development of novel bionanomaterials. Both experimental and theoretical studies on peptide self-assembly have shown that the self-assembly process spans multiple time and length scales and is hierarchical. β-sheet self-assembly consists of three sub-processes from the microscopic to the mesoscopic level: β-sheet locking, lateral stacking, and morphological transformation. Detailed atomistic simulation studies have provided insight into the early stages of peptide nanostructure formation and the interplay between different non-covalent interactions at the microscopic level. This review gives a brief introduction of the hierarchical peptide self-assembly process and focuses on the roles of various non-covalent interactions in the sub-processes based on recent simulation, experimental, and theoretical studies.

收稿时间:2015-04-30

Hierarchical processes in β -sheet peptide self-assembly from the microscopic to the mesoscopic level
Institution:Centre for Bioengineering and Biotechnology, China University of Petroleum (East China), Qingdao 266580, China
Abstract:Under appropriate physicochemical conditions, short peptide fragments and their synthetic mimics have been shown to form elongated cross-β nanostructures through self-assembly. The self-assembly process and the resultant peptide nanostructures are not only related to neurodegenerative diseases but also provide inspiration for the development of novel bionanomaterials. Both experimental and theoretical studies on peptide self-assembly have shown that the self-assembly process spans multiple time and length scales and is hierarchical. β -sheet self-assembly consists of three sub-processes from the microscopic to the mesoscopic level: β -sheet locking, lateral stacking, and morphological transformation. Detailed atomistic simulation studies have provided insight into the early stages of peptide nanostructure formation and the interplay between different non-covalent interactions at the microscopic level. This review gives a brief introduction of the hierarchical peptide self-assembly process and focuses on the roles of various non-covalent interactions in the sub-processes based on recent simulation, experimental, and theoretical studies.
Keywords:peptide  self-assembly  hierarchical process  nanostructures  
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