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Effect of bioactive glass crystallization on the conformation and bioactivity of adsorbed proteins
Author(s) -
Buchanan Laura A.,
ElGhannam Ahmed
Publication year - 2010
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.32561
Subject(s) - amide , protein adsorption , adsorption , adhesion , bovine serum albumin , crystallization , fourier transform infrared spectroscopy , fibronectin , materials science , cell adhesion , biomaterial , biophysics , chemistry , chemical engineering , cell , biochemistry , organic chemistry , biology , nanotechnology , composite material , engineering
Protein adsorption onto the surface of a biomaterial mediates cell adhesion and enhances tissue‐implant integration. In a previous study, we demonstrated that crystallization of bioactive glass (BG) significantly increased the negative zeta potential and decreased serum protein adsorption onto the material surface. In this study, the conformation of protein adsorbed onto the surface of amorphous bioactive glass (ABG) and crystallized bioactive glass (CBG) was analyzed and correlated to bone marrow mesenchymal stem cell adhesion and spreading. ABG and CBG were immersed in three different protein solutions containing 10% fetal bovine serum, bovine serum albumin (BSA), and fibronectin (FN) for 4 h at 37°C. Grazing angle Fourier transform infrared spectroscopy (GA‐FTIR) demonstrated that the ratio of (amide I)/(amide II) functional groups of all proteins adsorbed onto ABG was greater than that for proteins adsorbed onto CBG. The Gaussian curve fitting analysis suggests that the significant expression of amide I, rich in charged and flexible unordered secondary structure of adsorbed FN, stimulated bone cell adhesion and spreading on the surface of ABG. CBG enforces protein conformation that exposes amide II, rich in neutral and stable β‐sheet structure and α‐helix, which limited cell adhesion and spreading. Although ABG adsorbed significantly higher quantity of BSA than FN, GA‐FTIR analyses showed that the ratio of amide I/amide II was significantly higher for adsorbed FN. Therefore, the intensity of amide I or amide II bands cannot be taken as a measure of the quantity of adsorbed protein. © 2009 Wiley Periodicals, Inc. J Biomed Mater Res, 2010