中国科学院理论物理研究所机构知识库
Advanced  
ITP OpenIR  > 理论物理所2013年知识产出  > 期刊论文
题名: Tuning the Self-Assembly of Short Peptides via Sequence Variations
作者: Zhao, YR ;  Wang, JQ ;  Deng, L ;  Zhou, P ;  Wang, SJ ;  Wang, YT ;  Xu, H ;  Lu, JR
刊名: LANGMUIR
出版日期: 2013
卷号: 29, 期号:44, 页码:13457-13464
关键词: PARTICLE MESH EWALD ;  BIOMIMETIC SYNTHESIS ;  POTENTIAL FUNCTIONS ;  SILICA NANOTUBES ;  NANOSTRUCTURES ;  AMPHIPHILES ;  MOLECULES ;  ANTIBACTERIAL ;  MEMBRANE ;  POLYMERS
学科分类: Physics
通讯作者: Xu, H (reprint author), China Univ Petr East China, Ctr Bioengn & Biotechnol, 66 Changjiang West Rd, Qingdao 266580, Peoples R China.
部门归属: [Zhao, Yurong; Wang, Jiqian; Deng, Li; Zhou, Peng; Wang, Shengjie; Xu, Hai] China Univ Petr East China, Ctr Bioengn & Biotechnol, Qingdao 266580, Peoples R China; [Deng, Li; Wang, Yanting] Chinese Acad Sci, Inst Theoret Phys, State Key Lab Theoret Phys, Beijing 100190, Peoples R China; [Lu, Jian R.] Univ Manchester, Sch Phys & Astron, Biol Phys Grp, Manchester M13 9PL, Lancs, England
英文摘要: Peptide self-assembly is of direct relevance to protein science and bionanotechnology, but the underlying mechanism is still poorly understood. Here, we demonstrate the distinct roles of the noncovalent interactions and their impact on nanostructural templating using carefully designed hexapeptides, I2K2I2, I4K2, and KI4K. These simple variations in sequence led to drastic changes in final self-assembled structures, beta-sheet hydrogen bonding was found to favor the formation of one-dimensional nanostructures, such as nano-fibrils from I4K2 and nanotubes from KI4K, but the lack of evident beta-sheet hydrogen bonding in the case of I2(K2)I(2) led to no nanostructure formed. The lateral stacking and twisting of the beta-sheets were well-linked to the hydrophobic and electrostatic interactions between amino acid side chains and their interplay. For I4K2, the electrostatic repulsion acted to reduce the hydrophobic attraction between beta-sheets, leading to their limited lateral stacking and more twisting, and final fibrillar structures; in contrast, the repulsive force had little influence in the case of KI4K, resulting in wide ribbons that eventually developed into nanotubes. The fibrillar and tubular features were demonstrated by a combination of cryogenic transmission electron microscopy (cryo-TEM), negative-stain transmission electron microscopy (TEM), and small-angle neutron scattering (SANS). SANS also provided structural information at shorter scale lengths. All atom molecular dynamics (MD) simulations were used to suggest possible molecular arrangements within the beta-sheets at the very early stage of self-assembly.
资助者: National Natural Science Foundation of China [21033005, 91227115]; Natural Science Funds of Shandong Province of China for Distinguished Young Scholar [JQ201105]; National Science Foundation for Postdoctoral Scientists of China [2012M511555]; U.K. Engineering and Physical Sciences Research Council (EPSRC)
收录类别: SCI
原文出处: 查看原文
语种: 英语
WOS记录号: WOS:000326711200018
Citation statistics: 
内容类型: 期刊论文
URI标识: http://ir.itp.ac.cn/handle/311006/15243
Appears in Collections:理论物理所2013年知识产出 _期刊论文

Files in This Item: Download All
File Name/ File Size Content Type Version Access License
Tuning the Self-Assembly of Short Peptides via Sequence Variations.pdf(1081KB)----开放获取View Download

Recommended Citation:
Zhao, YR,Wang, JQ,Deng, L,et al. Tuning the Self-Assembly of Short Peptides via Sequence Variations[J]. LANGMUIR,2013,29(44):13457-13464.
Service
 Recommend this item
 Sava as my favorate item
 Show this item's statistics
 Export Endnote File
Google Scholar
 Similar articles in Google Scholar
 [Zhao, YR]'s Articles
 [Wang, JQ]'s Articles
 [Deng, L]'s Articles
CSDL cross search
 Similar articles in CSDL Cross Search
 [Zhao, YR]‘s Articles
 [Wang, JQ]‘s Articles
 [Deng, L]‘s Articles
Related Copyright Policies
Null
Social Bookmarking
  Add to CiteULike  Add to Connotea  Add to Del.icio.us  Add to Digg  Add to Reddit 
文件名: Tuning the Self-Assembly of Short Peptides via Sequence Variations.pdf
格式: Adobe PDF
此文件暂不支持浏览
所有评论 (0)
暂无评论
 
评注功能仅针对注册用户开放,请您登录
您对该条目有什么异议,请填写以下表单,管理员会尽快联系您。
内 容:
Email:  *
单位:
验证码:   刷新
您在IR的使用过程中有什么好的想法或者建议可以反馈给我们。
标 题:
 *
内 容:
Email:  *
验证码:   刷新

Items in IR are protected by copyright, with all rights reserved, unless otherwise indicated.

 

 

Valid XHTML 1.0!
Copyright © 2007-2017  中国科学院理论物理研究所 - Feedback
Powered by CSpace