Structure Characterization of Silk Fibroin Crystalline Domain Polypeptides Expressed in Escherichia coli  

作　　者：王建南 闫书芹 白伦 

机构地区：[1]National Engineering Laboratory for Modern Silk,Soochow University [2]College of Textile and Clothing Engineering,Soochow University

出　　处：《Journal of Donghua University(English Edition)》2011年第1期1-4,共4页东华大学学报（英文版）

基　　金：National Natural Science Foundation of China (No. 51075422);Natural Science Foundation of Jiangsu Province,China(No. BK2009147,No. BK2010253);Society Development Foundation of Suzhou City,China (No. SYG201001);the Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD)

摘　　要：The molecular conformations of four silk fibroin crystalline analogues [GAGAG-X] 16(G,Gly;A,Ala;X=Ala,Ser,Tyr or Val,designated eGA,eGS,eGY or eGV),carried out using molecular design and expressed by Escherichia coil(E.coli),were evaluated by Raman spectra analysis.The abilities of forming β-sheet structure were determined by thioflavin T(ThT) fluorescence spectra analysis.In terms of molecular conformation,except eGY that could not form significant typical molecular conformation,eGS and eGV were mainly composed of β-sheets while eGA tended to form β-turn.β-turn was also present in eGY and absent in eGS and eGV.In terms of β-sheet structure,eGS had the highest β-sheet content,followed by eGV,and eGA had the lowest content,furthermore,β-sheet structures were more stable in eGS and eGV than those in eGA and eGY.The molecular conformations of four silk fibroin crystalline analogues [GAGAG-X] 16（G,Gly;A,Ala;X=Ala,Ser,Tyr or Val,designated eGA,eGS,eGY or eGV）,carried out using molecular design and expressed by Escherichia coil（E.coli）,were evaluated by Raman spectra analysis.The abilities of forming β-sheet structure were determined by thioflavin T（ThT） fluorescence spectra analysis.In terms of molecular conformation,except eGY that could not form significant typical molecular conformation,eGS and eGV were mainly composed of β-sheets while eGA tended to form β-turn.β-turn was also present in eGY and absent in eGS and eGV.In terms of β-sheet structure,eGS had the highest β-sheet content,followed by eGV,and eGA had the lowest content,furthermore,β-sheet structures were more stable in eGS and eGV than those in eGA and eGY.

关 键 词：fibroin crystalline combination polypeptide Β-SHEET thioflavin T(ThT) Raman spectra 

分 类 号：TS146[轻工技术与工程—纺织材料与纺织品设计]