Self-assembled Monolayers of Methyl 1-thiahexa(ethylene oxide) for the Inhibition of Protein Adsorption

Published

June 11, 2002

Author(s)

David J. Vanderah, Gintaras Valincius, Curtis W. Meuse

Abstract

Self-assembled monolayers (SAMs) of methyl 1-thiahexa(ethylene oxide) [HS(CH₂CH₂O)₆CH₃] on gold were evaluated for their inhibition of non-specific protein adsorption (NSPA). Reflection-adsorption infrared spectroscopy (RAIRS) data of the HS(CH₂CH₂O)₆CH₃ SAMs showed that the 1-thiahexa(ethylene oxide) segment adopts the well ordered 7/2 helical conformation of the folded-chain crystal (FCC) polymorph of poly(ethylene oxide) upon assembly from 95% and 100% ethanol. Less ordered SAMs of HS(CH₂CH₂O)₆CH₃ were obtained upon assembly from tetrahydrofuran (THF), which RAIRS data indicateed are mixtures of the FCC and disordered conformations. Exposure of these surfaces to bovine serum albumin (BSA) and lysozyme solutions showed that the less ordered HS(CH₂CH₂O)₆CH₃ SAMs from THF exhibit better inhibition of NSPA. Thus the inhibition of NSPA of oligo(ethylene oxide) and methoxy-capped oligo(ethylene oxide) SAM surfaces cannot be attributed to highly ordered, helical conformations.

Citation

Langmuir

Volume

18

Issue

12

Pub Type

Journals

Keywords

oligo (ethylene oxides), protein adsorption, self-assembled monolayers

Citation

Ross, D. , Valincius, G. and Meuse, C. (2002), Self-assembled Monolayers of Methyl 1-thiahexa(ethylene oxide) for the Inhibition of Protein Adsorption, Langmuir (Accessed January 19, 2025)