Abstract:
:Silk fibroin exists in a number of different states, such as silk I and silk II, with different properties largely defined by differences in secondary structure composition. Numerous attempts have been made to control the transitions from silk I to silk II in vitro to produce high-performance materials. Of all the factors influencing the structural compositions, pH and some metal ions play important roles. This paper focuses on the influence of pH and Ca(2+) ions on the conformational transition from silk I to silk II in regenerated (redissolved) Bombyx mori fibroin. One- and two-dimensional correlation Raman spectroscopy was used to describe qualitatively the transitions in secondary structure in silk I, silk II, and their intermediates as pH and Ca(2+) ion concentration were changed, while (13)C cross polarization magic angle spinning (CP/MAS) solid-state NMR was used to quantify these changes. We showed that conditions (low pH, pH 5.2; a defined range of Ca(2+) ion concentrations; gradual water removal) that mimic natural silk spinning promote the formations of beta-sheet and distorted beta-sheet characteristic of silk II or silk II-related intermediate. In contrast, higher pH (pH 6.9-8.0) and higher Ca(2+) ion concentrations maintain "random coil" conformations typical of silk I or silk I-related intermediate. These results help to explain why the natural silk spinning process is attended by a reduction in pH from 6.9 to 4.8 and a change in the Ca(2+) ion concentration in the gland lumen as fibroin passes from the posterior division through the secretory pathway to the anterior division.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Zhou P,Xie X,Knight DP,Zong XH,Deng F,Yao WHdoi
10.1021/bi049344isubject
Has Abstractpub_date
2004-09-07 00:00:00pages
11302-11issue
35eissn
0006-2960issn
1520-4995journal_volume
43pub_type
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