A Survey of Structure−Property Relationships of Surfaces that Resist the Adsorption of Protein

TLDR

The study uses surface plasmon resonance spectroscopy and self‑assembled monolayers to identify functional groups that enable surfaces to resist nonspecific protein adsorption. Mixed SAMs were prepared by reacting organic amines with carboxylic anhydride‑terminated monolayers, and their protein‑resistance properties were screened by SPR. Surfaces incorporating oligo(sarcosine), N‑acetylpiperazine, or permethylated sorbitol groups showed strong protein resistance, comparable to but slightly inferior to oligo(ethylene glycol) monolayers, and were characterized by hydrophilicity, hydrogen‑bond acceptor functionality, and overall electrical neutrality.

Abstract

This paper describes the use of surface plasmon resonance (SPR) spectroscopy and self-assembled monolayers (SAMs) to determine the characteristics of functional groups that give surfaces the ability to resist the nonspecific adsorption of proteins from solution. Mixed SAMs presenting different functional groups were prepared for screening using a synthetic protocol based on the reaction of organic amines with a SAM terminated by interchain carboxylic anhydride groups. Surfaces that presented derivatives of oligo(sarcosine), N-acetylpiperazine, and permethylated sorbitol groups were particularly effective in resisting the adsorption of proteins. Incorporation of these groups into single-component SAMs resulted in surfaces that are comparable to (but slightly less good than) single-component SAMs that present oligo(ethylene glycol) in their ability to resist the adsorption of proteins. In the group of surfaces examined, those that resisted the adsorption of proteins had the following properties: they were hydrophilic; they contained groups that were hydrogen-bond acceptors but not hydrogen-bond donors; and they were overall electrically neutral.