Silica condensation by a silicatein α homologue involves surface-induced transition to a stable structural intermediate forming a saturated monolayer.

Abstract:

:Silicatein α exists within the protein filament of silica spicules of the marine sponge Tethya aurantium in a predominantly β-sheet structure. However, it is produced in a soluble form with mixed α-helix/β-sheet structure akin to its cathepsin L homologue. To understand this conformational transition in the context of enzyme catalyzed silica condensation, we used a functional, recombinant silicatein α termed 4SER. In solution, 4SER becomes conformationally unstable at pH 7 and readily unfolds to a soluble β-sheet intermediate, losing the majority of its helical structure. This β-sheet intermediate is present following adsorption of 4SER to a silica surface from solution. 4SER is particularly surface active, forming a near saturated monolayer on SiO2 from low bulk concentrations, without transition to multilayers at high bulk concentrations. The adsorbed intermediate remains stable during silica condensation and drying. We propose that the β-sheet structure for silicatein α in marine sponge spicules represents a stable structural intermediate, formed upon adsorption to the silica surface.

journal_name

Biomacromolecules

journal_title

Biomacromolecules

authors

Patwardhan SV,Holt SA,Kelly SM,Kreiner M,Perry CC,van der Walle CF

doi

10.1021/bm100932e

subject

Has Abstract

pub_date

2010-11-08 00:00:00

pages

3126-35

issue

11

eissn

1525-7797

issn

1526-4602

journal_volume

11

pub_type

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