title: [Effect of salt on minor ampullate silk spidroin modules].
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.
authors.forename: Jia
authors.initials: J
authors.lastname: Wang
authors.forename: Gefei
authors.initials: G
authors.lastname: Chen
authors.forename: Qing
authors.initials: Q
authors.lastname: Meng
mesh_terms: D000818:Animals; D005349:Fibroins / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012492:Salts / Q000737:chemistry*; D013112:Spiders
chemical_list: D012492:Salts; D005349:Fibroins