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In-Situ Characterization of Oligoethyleneoxide Self-Assembled Monolayers: Prospects for Protein Adsorption Resistance

Published

Author(s)

Marlon L. Walker, David J. Vanderah, Kenneth A. Rubinson

Abstract

In-situ spectroscopic ellipsometry was used to examine the adsorption of self-assembled monolayers (SAMs) of HS(CH2)3O(CH2CH2O)5CH3 C3(EO)5}, HS(CH2CH2O)6CH3 (EO)6}, and [S(CH2CH2O)6CH3]2 [S(EO)6]2} from aqueous solution onto Au substrates. The adsorption characteristics of the two thiol compounds were similar. The behavior of the disulfide compound, however, was clearly different, both in the adsorption profile and limiting thickness. Contact angle measurements indicate the disulfide surface is the most hydrophilic of those involved in this study. Bovine serum albumin adsorption studies on [S(EO)6]2 showed dramatic reduction of the amount of adsorbed protein on the disulfide surface compared to surfaces of bare Au and SAMs of octadecane thiol (ODT), C3(EO)5 and HS(EO)6. These results support the premise that surface-bound, conformationally mobile molecular chains of hydrophilic SAMs are needed for surface protein adsorption resistance.
Citation
Colloids and Surfaces B-Biointerfaces

Keywords

in-situ spectroscopic ellipsometry, oligo (ethylene oxide) disulfides, protein resistance, self-assembled monolayers

Citation

Walker, M. , Vanderah, D. and Rubinson, K. (2017), In-Situ Characterization of Oligoethyleneoxide Self-Assembled Monolayers: Prospects for Protein Adsorption Resistance, Colloids and Surfaces B-Biointerfaces (Accessed April 24, 2024)
Created February 19, 2017