Human Serum Albumin on Fluorinated Surfaces

The aim of this work is to investigate the stabilization of the conformation of adsorbed human serum albumin (HSA) on surfaces containing CF<INF>3</INF> and/or OH groups. These groups are structural characteristics (mimics) of trifluoroethanol, which is known to stabilize the secondary structure of several proteins. We focused on three different types of organic surfaces: (i) self-assembled monolayers (SAMs) prepared from mixtures of thiols with CF<INF>3</INF> and OH end groups, (ii) polymer surfaces of a poly(vinyl methyl ketone) (PVMK<INF>CF</INF><INF></INF><INFINF>3</INFINF><INF>/OH</INF>), which was modified with OH and CF<INF>3</INF> groups, and (iii) surfaces of polymer fluorosurfactant complexes containing CF<INF>3</INF> groups. It was revealed that the secondary structure of HSA in contact with the SAMs depends on the thiol composition. SAMs of mixed monolayers displayed the highest HSA recognition measured by antibody binding. CD measurements showed that PVMK<INF>CF</INF><INF></INF><INFINF>3</INFINF><INF>/OH</INF> surfaces retain the secondary structures of adsorbed HSA. Examples of polymer fluorosurfactant complexes are given that retain the secondary structure of adsorbed HSA and a complex that increase the content of α-helices. A combination of CF<INF>3</INF> and OH groups is proposed as a new approach to prepare biocompatible surfaces.