Protein Adsorption on Alkanethiolate Self-Assembled Monolayers:  Nanoscale Surface Structural and Chemical Effects

Citation

Li, Lingyan; Chen, Shengfu; & Jiang, Shaoyi (2003). Protein Adsorption on Alkanethiolate Self-Assembled Monolayers:  Nanoscale Surface Structural and Chemical Effects. Langmuir, 19(7), 2974-2982.

Abstract

We report a study of protein adsorption on controlled surfaces. Hydrophilic (carboxylic acid-terminated) and hydrophobic (methyl-terminated) self-assembled monolayers (SAMs) on Au(111) surfaces were prepared at different solution temperatures and characterized by low-current scanning tunneling microscopy (STM). Protein adsorption on these SAMs was investigated by surface plasmon resonance (SPR) sensors and tapping-mode atomic force microscopy (TM-AFM). Results show that both nanoscale surface chemical and structural properties of SAMs affect protein adsorption. Specifically, carboxylic acid-terminated SAMs formed at higher temperatures have more compact structures and generally promote protein adsorption, whereas the adsorbed amount of protein is similar on methyl-terminated SAMs regardless of solution temperatures at which SAMs are formed.

Reference Type

Journal Article

Secondary Title

Langmuir

Author(s)

Li, Lingyan
Chen, Shengfu
Jiang, Shaoyi

Year Published

2003

Date Published

1049155200

Volume Number

19

Issue Number

7

Pages

2974-2982

DOI

Protein Adsorption on Alkanethiolate Self-Assembled Monolayers10.1021/la0262957