The role of formic acid in solution stability and crystallization of silk protein polymer

被引:148
作者
Um, IC
Kweon, HY
Lee, KG
Park, YH [1 ]
机构
[1] Seoul Natl Univ, Dept Nat Fiber Sci, Suwon 441744, South Korea
[2] Natl Inst Agr Sci & Technol, Dept Sericulture & Entomol, Suwon 441100, South Korea
关键词
silk fibroin; formic acid; solution stability; crystallization;
D O I
10.1016/j.ijbiomac.2003.08.004
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In this paper. the regenerated silk fibroin (SF) solution dissolved in formic acid was used as a model protein to understand the role of formic acid in solution stability and crystallization of protein-based materials. The molecular decomposition of SF did not occur for the dissolution process in formic acid within 1-2 days of storage times. The P-sheet crystallization of SF molecules was occurred by the elimination of formic acid upon drying. The SF molecules in formic acid solution are stable and have low hydrodynamic radius values. This may be closely related to the fact that formic acid has two opposite functions of dissolution and crystallization simultaneously. The turbidity, dynamic light scattering and FTIR measurements elucidate that the solution stability and crystallization of SF are attributed to compact molecular shape of SF in formic acid, resulted from the molecular interactions between formic acid and polar groups in SF molecules. (C) 2003 Elsevier B.V. All rights reserved.
引用
收藏
页码:203 / 213
页数:11
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