The interaction of human serum albumin with titanium studied by means of atomic force microscopy

• Published in: Surface and interface analysis 2008-03, Vol.40 (3-4), p.157-161
• Main Authors: Van De Keere, Isabel, Willaert, Ronnie, Tourwé, Els, Hubin, Annick, Vereecken, Jean
• Format: Article
• Language: English
• Subjects: atomic force microscopy; biomaterial surfaces; Condensed matter: electronic structure, electrical, magnetic, and optical properties; Condensed matter: structure, mechanical and thermal properties; Cross-disciplinary physics: materials science; rheology; Exact sciences and technology; human serum albumin; Physics; protein adsorption; titanium
• ISSN: 0142-2421; 1096-9918
• DOI: 10.1002/sia.2673

Titanium is frequently used as a biomaterial for implants in orthopaedics and cardiovascular devices. Understanding the biocompatibility, which is strongly influenced by the adsorption of proteins onto the surface, is very important to improve implants. The surface chemistry of an implant material and its influence on the interaction with body fluid is crucial in that perspective. The main goal of this study was to investigate the conformation of human serum albumin (HSA) with commercially pure titanium (CP Ti) on a molecular level. Both ex situ and in situ AFM imaging showed the conformation of HSA on CP Ti and on mica, which was used as a reference material. Single molecules and aggregates of albumin were observed. HSA can be recognised by the globular shape. The conformation of the adsorbed HSA molecules was different on titanium and mica, for both the ex situ and in situ imaging. The difference in wettability between both substrates caused a larger spread of the protein on the CP Ti surface and thus resulted in a larger perturbation of the native structure of HSA as compared to mica. Copyright © 2008 John Wiley & Sons, Ltd.