Protein adsorption on low-temperature isotropic carbon: I. Protein conformational change probed by differential scanning calorimetry.

Abstract

This is the first of a set of articles on protein adsorption on low-temperature isotropic carbon (LTIC), a reputed blood compatible material. Surface-induced conformational changes of albumin, fibrinogen, and some small proteins were measured by differential scanning calorimetry (DSC) on LTIC powders and colloidal silica. The LTIC surface significantly alters the DSC response (denaturation?) in proteins studied in different buffer solutions. We use the term "denaturation" to refer to altered protein behavior in the adsorbed state. Hydrophobic interactions between LTIC and the proteins are thought to be the major driving force. The presence of air at the water-carbon interface seems to prevent the surface denaturation of fibrinogen. The silica surface greatly denatures albumin but only slightly denatures fibrinogen. Because LTIC is considered to be a nonthrombogenic material, but silica is considered to be a thrombogenic one, whether a surface denatures adsorbed proteins cannot be the sole criterion for its blood compatibility. The latter largely depends on what protein the surface denatures, and in what sequences.