| Literature DB >> 12767126 |
Chenhua Zhao1, Juming Yao, Hiromi Masuda, Raghuvansh Kishore, Tetsuo Asakura.
Abstract
High-resolution solution (13)C-NMR and CD studies of Bombyx mori silk fibroin revealed the presence of an ordered secondary structure 3(10)-helix, in hexafluoro-iso-propanol (HFIP). The solid-state structure of the silk fibroin film prepared by drying it gently from the HFIP solution still keep the structure, 3(10)-helix, which was studied with high-resolution solid state (13)C-NMR. The structural transition from the 3(10)-helix to silk II structure, heterogeneous structure including antiparallel beta-sheet, occurred during the artificial spinning from the HFIP solution. The wide-angle x-ray diffraction and differential scanning calorimetry thermograms of the artificial spinning fiber after postspinning treatments were observed together with the stress-strain curves. The results emphasize that the molecular structures, controlled morphology, and mechanical properties of the protein-based synthetic polymers can be modulated for enhancing biocompatibility. Copyright 2003 Wiley Periodicals, Inc.Entities:
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Year: 2003 PMID: 12767126 DOI: 10.1002/bip.10350
Source DB: PubMed Journal: Biopolymers ISSN: 0006-3525 Impact factor: 2.505