中国物理B ›› 2016, Vol. 25 ›› Issue (1): 18701-018701.doi: 10.1088/1674-1056/25/1/018701

所属专题: TOPICAL REVIEW — 8th IUPAP International Conference on Biological Physics

• TOPICAL REVIEW—8th IUPAP International Conference on Biological Physics • 上一篇    下一篇

Hierarchical processes in β -sheet peptide self-assembly from the microscopic to the mesoscopic level

Li Deng(邓礼) and Hai Xu(徐海)   

  1. Centre for Bioengineering and Biotechnology, China University of Petroleum (East China), Qingdao 266580, China
  • 收稿日期:2015-04-30 修回日期:2015-07-03 出版日期:2016-01-05 发布日期:2016-01-05
  • 通讯作者: Hai Xu E-mail:xuh@upc.edu.cn
  • 基金资助:

    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).

Hierarchical processes in β -sheet peptide self-assembly from the microscopic to the mesoscopic level

Li Deng(邓礼) and Hai Xu(徐海)   

  1. Centre for Bioengineering and Biotechnology, China University of Petroleum (East China), Qingdao 266580, China
  • Received:2015-04-30 Revised:2015-07-03 Online:2016-01-05 Published:2016-01-05
  • Contact: Hai Xu E-mail:xuh@upc.edu.cn
  • Supported by:

    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.

关键词: peptide, self-assembly, hierarchical process, nanostructures

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.

Key words: peptide, self-assembly, hierarchical process, nanostructures

中图分类号:  (Fibrils (amyloids, collagen, etc.))

  • 87.14.em
87.14.ef (Peptides) 87.10.Tf (Molecular dynamics simulation) 87.10.Pq (Elasticity theory)