Issue 48, 2009
From the journal:

Chemical Communications

Two distinct β-sheet fibrils from silk protein†

Zuguang Gong,a   Lei Huang,a   Yuhong Yang,*b   Xin Chena  and  Zhengzhong Shao*a  

* Corresponding authors

a Key Laboratory of Molecular Engineering of Polymers of Ministry of Education, Laboratory of Advanced Materials, Department of Macromolecular Science, Fudan University, 220 Handan Road, Shanghai 200433, People’s Republic of China
E-mail: zzshao@fudan.edu.cn

b Research Center for Analysis and Measurement, Fudan University, 220 Handan Road, Shanghai 200433, People’s Republic of China
E-mail: yuhongyang@fudan.edu.cn

Abstract

This study showed that Bombyx mori silk protein could be selectively induced to fold into fibrils dominated by either cross- or parallel-β-sheet structure, where the β-strands arrange perpendicular or parallel to the long fibril axis, incubated in ethanol–water quiescently or in water under shear.

Graphical abstract: Two distinct β-sheet fibrils from silk protein

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Article information

DOI
https://doi.org/10.1039/B914218E
Article type
Communication
Submitted
15 Jul 2009
Accepted
23 Oct 2009
First published
12 Nov 2009

Chem. Commun., 2009, 7506-7508

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Two distinct β-sheet fibrils from silk protein

Z. Gong, L. Huang, Y. Yang, X. Chen and Z. Shao, Chem. Commun., 2009, 7506 DOI: 10.1039/B914218E

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