Effect of salt on minor ampullate silk spidroin modules.
- Author:
Jia WANG
;
Gefei CHEN
;
Qing MENG
- Publication Type:Journal Article
- MeSH:
Animals;
Fibroins;
chemistry;
Protein Structure, Secondary;
Salts;
chemistry;
Spiders
- From:
Chinese Journal of Biotechnology
2014;30(8):1308-1317
- CountryChina
- Language:Chinese
-
Abstract:
To study the effect of physiological conditions on spidroins, we analyzed NTR1SR2CT module secondary structure, aggregation and silk-formation influenced by different salts (in different concentration intervals). According to the full-length Araneus ventricosus MiSp sequence, NTR1SR2CT module was constructed and expressed in Escherichia coli BL21 (DE3), and the recombinant proteins were purified by denaturation method mediated by 8 mol/L urea. Random coil and helix are the main secondary structures of NTR1SR2CT and could be induced into beta-sheet by drying natively and lyophilization, where methanol can be used as a promoter. Furthermore, potassium and phosphate cations can cause significant NTR1SR2CT protein aggregation and silk-formation. The results could be a basis for the determination of silk-formation mechanism, and also useful for industrialized generation of high performance spider silk-like fibers.
