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Structural characterization and artificial fiber formation of Bombyx mori silk fibroin in hexafluoro‐iso‐propanol solvent system
Author(s) -
Zhao Chenhua,
Yao Juming,
Masuda Hiromi,
Kishore Raghuvansh,
Asakura Tetsuo
Publication year - 2003
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10350
Subject(s) - fibroin , bombyx mori , silk , chemistry , differential scanning calorimetry , polymer chemistry , chemical engineering , protein secondary structure , solvent , crystallography , helix (gastropod) , materials science , composite material , organic chemistry , biochemistry , physics , gene , engineering , thermodynamics , ecology , biology , snail
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 β‐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. © 2003 Wiley Periodicals, Inc. Biopolymers 69: 253–259, 2003