Mussel adhesive protein inspired coatings: a versatile method to fabricate silica films on various surfaces

Rai, A and Perry, CC ORCID: https://orcid.org/0000-0003-1517-468X, 2012. Mussel adhesive protein inspired coatings: a versatile method to fabricate silica films on various surfaces. Journal of Materials Chemistry, 22 (11), pp. 4790-4796. ISSN 0959-9428

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Abstract

A simple and versatile biomimetic strategy for the fabrication of silica films on a variety of substrates including gold, polystyrene and silicon wafers was developed using nanogram amounts per cm 2 of silicatein. The strategy exploits the adhesive property of 3,4-dihydroxyphenylalanine (DOPA) and a decapeptide (Ala-Lys-Pro-Ser-Tyr-DHP-Hyp-Thr-DOPA-Lys), important components of mussel adhesive proteins, to modify the surface of substrates. DOPA molecules polymerize to poly(DOPA) and the decapeptide forms thin films on gold substrates at pH 8.5, rendering the substrate compatible for silicatein immobilization. Nearly 50 ng cm 2 of silicatein is immobilized on poly(DOPA) and decapeptide coated surfaces where these polymer films act as "cushion" to protect the active structure and maintain the activity of the largely chemically adsorbed silicatein at ca. 95% of that experienced in solution. Uniform silica films of thickness 130-140 nm and roughness 12-14.5 nm were fabricated on coated gold surfaces. Evidence to show that this method is also applicable for the fabrication of uniform silica films on polystyrene and silicon substrates over multiple length scales in an economical way is also presented.

Item Type:	Journal article
Publication Title:	Journal of Materials Chemistry
Creators:	Rai, A. and Perry, C.C.
Publisher:	Royal Society of Chemistry
Date:	2012
Volume:	22
Number:	11
ISSN:	0959-9428
Identifiers:	Number Type 10.1039/c2jm15810h DOI
Rights:	© Royal Society of Chemistry 2012
Divisions:	Schools > School of Science and Technology
Record created by:	EPrints Services
Date Added:	09 Oct 2015 10:38
Last Modified:	09 Jun 2017 13:35
URI:	https://irep.ntu.ac.uk/id/eprint/15941

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