Premium
The interaction of human serum albumin with titanium studied by means of atomic force microscopy
Author(s) -
Van De Keere Isabel,
Willaert Ronnie,
Tourwé Els,
Hubin Annick,
Vereecken Jean
Publication year - 2008
Publication title -
surface and interface analysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.52
H-Index - 90
eISSN - 1096-9918
pISSN - 0142-2421
DOI - 10.1002/sia.2673
Subject(s) - mica , titanium , biocompatibility , biomaterial , human serum albumin , wetting , adsorption , protein adsorption , chemistry , molecule , albumin , atomic force microscopy , globular protein , contact angle , chemical engineering , nanotechnology , biophysics , crystallography , materials science , biochemistry , organic chemistry , composite material , engineering , biology
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.