Principles Governing Catalytic Activity of Self-Assembled Short Peptides

doi:10.1021/jacs.8b08893

	Principles Governing Catalytic Activity of Self-Assembled Short Peptides
	Song, Ruiheng 1; Wu, Xialian2,4 ; Xue, Bin 3; Yang, Yuqin 1; Huang, Wenmao 3; Zeng, Guixiang 1,5; Wang, Jian2 ; Li, Wenfei 3,5; Cao, Yi 3,5; Wang, Wei 3,5; Lu, Junxia2 ; Dong, Hao 1,5
	2019-01-09
发表期刊	JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (IF:14.4[JCR-2023],14.8[5-Year])
ISSN	0002-7863
卷号	141 期号:1 页码:223-231
发表状态	已发表
DOI	10.1021/jacs.8b08893
摘要	Molecular self-assembly provides a chemical strategy for the synthesis of nanostructures by using the principles of nature, and peptides serve as the promising building blocks to construct adaptable molecular architectures. Recently, a series of heptapeptides with alternative hydrophobic and hydrophilic residues were reported to form amyloid-like structures, which are capable of catalyzing acyl ester hydrolysis with remarkable efficiency. However, information remains elusive about the atomic structures of the fibrils. What is the origin of the sequence-dependent catalytic activity? How is the ester hydrolysis catalyzed by the fibrils? In this work, the atomic structures of the aggregates were determined by using molecular modeling and further validated by solid-state NMR experiments, where the fibril with high activity adopts twisted parallel configuration within each layer, and the one with low activity is in flat antiparallel configuration. The polymorphism originates from the interactions between different regions of the building block peptides, where the delicate balance between rigidity and flexibility plays an important role. We further show that the p-nitrophenylacetate (pNPA) hydrolysis reactions catalyzed by two different fibrils follow a similar mechanism, and the difference in microenvironment at the active site between the natural enzyme and the present self-assembled fibrils should account for the discrepancy in catalytic activities. The present work provides understanding of the structure and function of self-assembled fibrils formed with short peptides at an atomic level and thus sheds new insight on designing aggregates with better functions.
收录类别	SCI ; SCIE ; EI
语种	英语
资助项目	Fundamental Research Funds for the Central Universities[021514380012] ; Fundamental Research Funds for the Central Universities[021514380014]
WOS研究方向	Chemistry
WOS类目	Chemistry, Multidisciplinary
WOS记录号	WOS:000455561800039
出版者	AMER CHEMICAL SOC
WOS关键词	CARBONIC-ANHYDRASE-II ; PROTON-TRANSFER ; SIDE-CHAINS ; BETA-SHEETS ; MECHANISM ; MODEL ; SIMULATIONS ; DYNAMICS ; COPPER ; PK(A)
原始文献类型	Article
引用统计	正在获取...
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/30157
专题	生命科学与技术学院_博士生生命科学与技术学院_PI研究组_陆珺霞组生命科学与技术学院_公共科研平台_分子细胞学平台
通讯作者	Wang, Wei; Lu, Junxia; Dong, Hao
作者单位	1.Nanjing Univ, Kuang Yarning Honors Sch, Nanjing 210023, Jiangsu, Peoples R China 2.ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai 201210, Peoples R China 3.Nanjing Univ, Collaborat Innovat Ctr Adv Microstruct, Dept Phys, Natl Lab Solid State Microstruct, Nanjing 210093, Jiangsu, Peoples R China 4.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 5.Nanjing Univ, Inst Brain Sci, Nanjing 210023, Jiangsu, Peoples R China
通讯作者单位	生命科学与技术学院
推荐引用方式 GB/T 7714	Song, Ruiheng,Wu, Xialian,Xue, Bin,et al. Principles Governing Catalytic Activity of Self-Assembled Short Peptides[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,2019,141(1):223-231.
APA	Song, Ruiheng.,Wu, Xialian.,Xue, Bin.,Yang, Yuqin.,Huang, Wenmao.,...&Dong, Hao.(2019).Principles Governing Catalytic Activity of Self-Assembled Short Peptides.JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,141(1),223-231.
MLA	Song, Ruiheng,et al."Principles Governing Catalytic Activity of Self-Assembled Short Peptides".JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 141.1(2019):223-231.