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Self-assembly and morphological characterization of two-component functional amyloid proteins
Qi, Qi2; Zhao, Tian-Xin; An, Bo-Lin; Liu, Xuan-Yong; Zhong, Chao
2017
Source PublicationCHINESE CHEMICAL LETTERS
ISSN1001-8417
Volume28Issue:5Pages:1062
AbstractFunctional amyloid has been increasingly applied as self-assembling nanostructures to construct multifunctional biomaterials. However, little has been known how different side domains, varied fusion positions and subunits affect self-assembly and morphologies of amyloid fibrils. Here, we constructed three groups of two-component amyloid proteins based on CsgA, the major protein components of Escherichia coli biofilms, to bridge these gaps. We showed that all fusion proteins have amyloid features, as indicated by Congo red assay. Atomic force microscopy (AFM) indeed reveals that these fusion proteins are able to self-assemble into fibrils, with an average diameter of 0.5-2 nm and length of hundreds of nanometers to several micrometers. The diameter of fibrils increases with the increase of the molecular weight of fusion domains, while the dynamic assembly of recombinant proteins was delayed as a result of the introduction of fusion domains. Moreover, fusion of the same functional domains but at intermediate position seems to cause the most interference on fibril assembly compared with those fused at C or N-terminus, as mainly short and irregular fibrils were detected. This phenomenon appears more pronounced for randomly coiled mussel foot proteins (Mfps) than for rigid chitin-binding domain (CBD). Finally, increase of the molecular weight of tandem repeats in protein monomer seemed to increase the fibril diameter of the resultant fibrils, but either reduction of the tandem repeats of CsgA to one single belta-sheet loop or increase in the number of tandem repeats of CsgAs from one to four produced shorter and intermittent fibrils compared with CsgA control protein. These studies therefore provide insights into self-assembly of two-component amyloid proteins and lay the foundation for rational design of multifunctional molecular biomaterials. (C) 2016 Chinese Chemical Society and Institute of Materia Medica, Chinese Academy of Medical Sciences. Published by Elsevier B.V. All rights reserved.
DOI10.1016/j.cclet.2016.12.008
WOS IDWOS:000402444600027
EI Accession Number1878-5964
Citation statistics
Cited Times:5[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.sic.ac.cn/handle/331005/26681
Collection中国科学院上海硅酸盐研究所
Affiliation1.ShanghaiTech Univ, Sch Phys Sci & Technol, Shanghai 200120, Peoples R China
2.Chinese Acad Sci, Shanghai Inst Ceram, Shanghai 200050, Peoples R China
3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
Recommended Citation
GB/T 7714
Qi, Qi,Zhao, Tian-Xin,An, Bo-Lin,et al. Self-assembly and morphological characterization of two-component functional amyloid proteins[J]. CHINESE CHEMICAL LETTERS,2017,28(5):1062.
APA Qi, Qi,Zhao, Tian-Xin,An, Bo-Lin,Liu, Xuan-Yong,&Zhong, Chao.(2017).Self-assembly and morphological characterization of two-component functional amyloid proteins.CHINESE CHEMICAL LETTERS,28(5),1062.
MLA Qi, Qi,et al."Self-assembly and morphological characterization of two-component functional amyloid proteins".CHINESE CHEMICAL LETTERS 28.5(2017):1062.
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