Tuning the Self-Assembly of Short Peptides via Sequence Variations

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	Tuning the Self-Assembly of Short Peptides via Sequence Variations
	Wang, YT
刊名	LANGMUIR
	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
ISSN号	0743-7463
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.
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.
学科主题	Physics
收录类别	SCI
资助信息	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)
原文出处	http://dx.doi.org/10.1021/la402441w
语种	英语
WOS记录号	WOS:000326711200018
公开日期	2014-04-25
内容类型	期刊论文
源URL	[http://ir.itp.ac.cn/handle/311006/15243]
专题	理论物理研究所_理论物理所1978-2010年知识产出
推荐引用方式 GB/T 7714	Wang, YT. Tuning the Self-Assembly of Short Peptides via Sequence Variations[J]. LANGMUIR,2013,29(44):13457-13464.
APA	Wang, YT.(2013).Tuning the Self-Assembly of Short Peptides via Sequence Variations.LANGMUIR,29(44),13457-13464.
MLA	Wang, YT."Tuning the Self-Assembly of Short Peptides via Sequence Variations".LANGMUIR 29.44(2013):13457-13464.