The Self-Assembly and Inhibition of Protein Adsorption by Thiolated Dextran Monolayers at Hydrophobic Metal Surfaces View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1996

AUTHORS

Richard A. Frazier , Martyn C. Davies , Gert Matthijs , Clive J. Roberts , Etienne Schacht , Simon Tasker , Saul J. B. Tendler

ABSTRACT

Dextran may be immobilized to a metal surface via thiol functionality introduced by chemical modification of hydroxyl groups on the polymer backbone. This paper details the characterization of thiolated dextrans, of molecular weights ranging 5 kDa to 500 kDa, chemisorbed to silver and their use as inhibitors of protein adsorption. Surface plasmon resonance (SPR) has been employed to monitor bovine serum albumin (BSA) adsorption from a flowing buffered solution. In addition, in situ SPR assays of any adsorbed BSA were carried out with anti-BSA antibody. The results obtained by SPR have been complemented and validated by ellipsometry, atomic force microscopy (AFM) and X-ray photoelectron spectroscopy (XPS) analysis. Whilst a significant reduction of BSA adsorption to dextran compared to the uncoated silver surface is observed, the degree of conversion of hydroxyls to thiol groups and molecular weight is seen to affect the nature and protein resistant performance of the dextran layer. By increasing the proportion of thiol substituents, a greater coverage is observed, conferring improved protein resistance. Higher molecular weight dextrans are shown to pack less efficiently to produce layers with less effective protein resistance. More... »

PAGES

117-127

Book

TITLE

Surface Modification of Polymeric Biomaterials

ISBN

978-1-4899-1955-7
978-1-4899-1953-3

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4899-1953-3_14

DOI

http://dx.doi.org/10.1007/978-1-4899-1953-3_14

DIMENSIONS

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