Secondary structure and dynamics study of the intrinsically disordered silica-mineralizing peptide P₅ S₃ during silicic acid condensation and silica decondensation.

ABSTRACT: The silica forming repeat R5 of sil1 from Cylindrotheca fusiformis was the blueprint for the design of P₅ S₃ , a 50-residue peptide which can be produced in large amounts by recombinant bacterial expression. It contains 5 protein kinase A target sites and is highly cationic due to 10 lysine and 10 arginine residues. In the presence of supersaturated orthosilicic acid P₅ S₃ enhances silica-formation whereas it retards the dissolution of amorphous silica (SiO₂ ) at globally undersaturated concentrations. The secondary structure of P₅ S₃ during these 2 processes was studied by circular dichroism (CD) spectroscopy, complemented by nuclear magnetic resonance (NMR) spectroscopy of the peptide in the absence of silicate.

SUBMITTER: Zerfaß C 

PROVIDER: S-EPMC5760248 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature