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学科主题基础医学
One-dimensional self-assembly of a rational designed beta-structure peptide
Wang, Chong; Huang, Lixin; Wang, Lijun; Hong, Yuankai; Sha, Yinlin
关键词peptide self-assembly peptide design AFM molecular modeling nanofibril tape beta-sheet
刊名BIOPOLYMERS
2007-05-01
DOI10.1002/bip.20681
86期:1页:23-31
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Biochemistry & Molecular Biology ; Biophysics
研究领域[WOS]Biochemistry & Molecular Biology ; Biophysics
关键词[WOS]AMYLOID FIBRIL FORMATION ; SIDE-CHAIN INTERACTIONS ; CIRCULAR-DICHROISM ; SMART MATERIALS ; SHEET PEPTIDE ; PROTEINS ; RIBBONS ; MODEL ; NANOTUBES ; ARCHITECTURE
英文摘要

Fabricating various nanostructures based on the self-assembley of diverse biological molecules is now of great interest to the field of bionanotechnol. In this study we report a de novo designed peptide (T1) with a preferential beta-hairpin forming property that curt spontaneously assemble into nanofibrils in ultrapure water. The nanofibrils assembled by T1 could grow up to tens of microns in length with a left-handed helical twist and an average height of 4.9 +/- 0.9 nm. Moreover, protofilaments and nucleus structures both with a similar height of 1.4 +/- 0.2 nm were observed during fibrilization as well as via sonication of the mature nanofibrils. A typical conformational transition from random coil to beta-structure was observed in association with the fibrilization. Molecular modeling of T1 assemblies displayed that the beta-hairpin molecules organize in a parallel fashion in which the beta-strands align in an antiparallel fashion and each adjoining beta-strand runs left-handed twist at about 2.9 degrees with respect to the one located before it along the fibrillar axis. It also revealed that the maximum thickness of the assembly intermediate, the helical tape structure, is about 1.4 nm and four tapes can further assemble into a fibril with a diameter of about 4.1 nm. Taken together the results obtained by AFM, CD, and molecular modeling, T1 fibrilization probably undergoes a hierarchy approach, in which the aromatic stacking and the electrostatic interactions between the assembled structures are most likely the two major factors directing the one-dimensional self-assembly. Based on these studies, we propose T1 can be used as a model peptide to investigate the beta-sheet based self-assembly process and could be a potential bioorganic template to develop functional materials. (c) 2007 Wiley Periodicals, Inc.

语种英语
WOS记录号WOS:000245874700003
引用统计
被引频次:13[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
版本出版稿
条目标识符http://ir.bjmu.edu.cn/handle/400002259/53520
专题北京大学基础医学院_生物物理学系
作者单位1.Peking Univ, Biomed X Ctr, Beijing 100083, Peoples R China
2.Peking Univ, Sch Basic Med Sci, Dept Biophys, Single Mol & Nanobiol Lab, Beijing 100083, Peoples R China
推荐引用方式
GB/T 7714
Wang, Chong,Huang, Lixin,Wang, Lijun,et al. One-dimensional self-assembly of a rational designed beta-structure peptide[J]. BIOPOLYMERS,2007,86(1):23-31.
APA Wang, Chong,Huang, Lixin,Wang, Lijun,Hong, Yuankai,&Sha, Yinlin.(2007).One-dimensional self-assembly of a rational designed beta-structure peptide.BIOPOLYMERS,86(1),23-31.
MLA Wang, Chong,et al."One-dimensional self-assembly of a rational designed beta-structure peptide".BIOPOLYMERS 86.1(2007):23-31.
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