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Principles Governing Catalytic Activity of Self-Assembled Short Peptides
2019-01-09
发表期刊JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (IF:14.4[JCR-2023],14.8[5-Year])
ISSN0002-7863
卷号141期号:1页码:223-231
发表状态已发表
DOI10.1021/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
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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
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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.
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