title: Influence of reaction conditions on the self-assembly of the natural silk sericin protein.
abstract: In the past years, the self-assembly of specific proteins has been paid more and more attention due to their significant role in human health and fabrication of new materials. In this article, we explore the effect of reaction conditions on the self-assembly of natural silk sericin protein, including the molecular weight and the concentration of sericin, pH, and metal ions in the reaction system. The results indicate that all these factors, especially species and concentration of metal ions, could influence the self-assembly process of the silk sericin protein. A series of assemblies with various morphologies can be fabricated by modulating the reaction condition. The article may provide some clue for the understanding of the protein self-assembly in the body and a method to fabricate new organic materials with different morphology. Microsc. Res. Tech. 80:298-304, 2017. © 2016 Wiley Periodicals, Inc.
authors.affiliation: The Key Laboratory of Advanced Textile Materials and Manufacturing Technology of Ministry of Education, National Engineering Lab for Textile Fiber Materials and Processing Technology, College of Materials and Textiles, Zhejiang Sci-Tech University, Hangzhou, 310018, China.
authors.forename: Wenhua
authors.initials: W
authors.lastname: Li
authors.affiliation: The Key Laboratory of Advanced Textile Materials and Manufacturing Technology of Ministry of Education, National Engineering Lab for Textile Fiber Materials and Processing Technology, College of Materials and Textiles, Zhejiang Sci-Tech University, Hangzhou, 310018, China.
authors.forename: Xiuping
authors.initials: X
authors.lastname: Su
authors.affiliation: The Key Laboratory of Advanced Textile Materials and Manufacturing Technology of Ministry of Education, National Engineering Lab for Textile Fiber Materials and Processing Technology, College of Materials and Textiles, Zhejiang Sci-Tech University, Hangzhou, 310018, China.
authors.forename: Qiwei
authors.initials: Q
authors.lastname: Zhong
authors.affiliation: The Key Laboratory of Advanced Textile Materials and Manufacturing Technology of Ministry of Education, National Engineering Lab for Textile Fiber Materials and Processing Technology, College of Materials and Textiles, Zhejiang Sci-Tech University, Hangzhou, 310018, China.
authors.forename: Zhaogang
authors.initials: Z
authors.lastname: Liu
authors.affiliation: The Key Laboratory of Advanced Textile Materials and Manufacturing Technology of Ministry of Education, National Engineering Lab for Textile Fiber Materials and Processing Technology, College of Materials and Textiles, Zhejiang Sci-Tech University, Hangzhou, 310018, China.
authors.forename: Yurong
authors.initials: Y
authors.lastname: Cai
authors.affiliation: The Key Laboratory of Advanced Textile Materials and Manufacturing Technology of Ministry of Education, National Engineering Lab for Textile Fiber Materials and Processing Technology, College of Materials and Textiles, Zhejiang Sci-Tech University, Hangzhou, 310018, China.
authors.forename: Juming
authors.initials: J
authors.lastname: Yao
mesh_terms: D000818:Animals; D001672:Biocompatible Materials / Q000737:chemistry*; D012831:Bombyx; D002122:Calcium Chloride / Q000737:chemistry; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000737:chemistry; D008422:Materials Testing / Q000379:methods; D008855:Microscopy, Electron, Scanning; D008970:Molecular Weight; D011487:Protein Conformation; D047030:Sericins / Q000737:chemistry* / Q000648:ultrastructure; D047011:Silk / Q000737:chemistry* / Q000648:ultrastructure; D017550:Spectroscopy, Fourier Transform Infrared; D015032:Zinc / Q000737:chemistry
chemical_list: D001672:Biocompatible Materials; D047030:Sericins; D047011:Silk; D008274:Magnesium; D015032:Zinc; D002122:Calcium Chloride
keywords: conformation transition; metal ions; self-assembly; silk sericin