Effects of plasma protein adsorption on protein conformation and activity

Abstract

Protein adsorption at solid-liquid interfaces may lead to significant changes in conformation. Such effects can be monitored in situ for native, unlabelled proteins using the total internal reflection spectroscopy method, by monitoring the UV fluorescence of tryptophan side chains at 320–350 nm. Such studies suggest a partial denaturation of human plasma fibronectin on hydrophobic silica and a blue shift for bovine albumin on hydrophilic silica. © 1984 IUPAC