Premium
On the role of CO 2 laser treatment in the human serum albumin and human plasma fibronectin adsorption on zirconia (MGO‐PSZ) bioceramic surface
Author(s) -
Hao L.,
Lawrence J.
Publication year - 2004
Publication title -
journal of biomedical materials research part a
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.849
H-Index - 150
eISSN - 1552-4965
pISSN - 1549-3296
DOI - 10.1002/jbm.a.30055
Subject(s) - adsorption , wetting , materials science , fibronectin , protein adsorption , cubic zirconia , chemical engineering , human serum albumin , albumin , contact angle , surface energy , blood proteins , surface roughness , ceramic , chromatography , organic chemistry , composite material , chemistry , biochemistry , cell , engineering
The nature of the surface strongly influences the composition and recognizability of the adsorbed protein layer, which in turn affects the subsequent cellular interactions. Thus, to understand the biological response to a material, especially in vitro , one must fully understand the nature of the adsorbed protein film that forms on the material. This study investigates the fundamental interactions between the human serum albumin (no‐cell adhesive) and human plasma fibronectin and bioinert ceramic following CO 2 laser treatment. The analysis of the albumin and fibronectin adsorption was conducted on the untreated and CO 2 laser‐modified magnesia partially stabilized zirconia (MgO‐PSZ) bioceramic using an ellipsometry. It was found that the adsorptions of albumin and fibronectin were influenced by the surface properties. The albumin adsorption was affected by the surface roughness and wettability characteristics of the MgO‐PSZ and decreased with these properties, while the fibronectin adsorption was increased with wettability characteristics and predominantly governed by this property. Moreover, the considerable change in the polar component of surface energy, γ sv p , and its effect on protein adsorption implied that the albumin and fibronectin adsorption on the MgO‐PSZ surfaces was probably due to the polar and chemical interactions. The value of this work is to provide a novel technique and useful information for manipulating protein adsorption and thereof cellular interactions. © 2004 Wiley Periodicals, Inc. J Biomed Mater Res 69A: 748–756, 2004