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Influence of surface features of hydroxyapatite on the adsorption of proteins relevant to bone regeneration
Author(s) -
FernándezMontes Moraleda Belén,
Román Julio San,
RodríguezLorenzo Luís M.
Publication year - 2013
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.34528
Subject(s) - adsorption , materials science , protein adsorption , amide , regeneration (biology) , fibronectin , specific surface area , chemical engineering , organic chemistry , biochemistry , chemistry , extracellular matrix , biology , engineering , microbiology and biotechnology , catalysis
Protein–surface interaction may determine the success or failure of an implanted device. Not much attention have been paid to the specific surface parametes of hydroxyapatite (OHAp) that modulates and determines the formation and potential activity of the layer of proteins that is first formed when the material get in contact with the host tissue. the influence of specific surface area (SSA), crystallite size (CS) and particle size (PS) of OHAp on the adsorption of proteins relevant for bone regeneration is evaluated in this article. OHAp have been prepared by a wet chemical reaction of Ca(OH) 2 with H 3 PO 4 . One set of reactions included poly acrylic acid in the reactant solution to modify the properties of the powder. Fibrinogen (Fg) Fraction I, type I: from Human plasma, (67% Protein), and Fibronectin (Fn) from Human plasma were selected to perform the adsorption experiments. The analysis of protein adsorption was carried out by UV/Vis spectrometry. A lower SSA and a different aspect ratio are obtained when the acrylic acid is included in the reaction badge. The deconvolution of the amide I band on the Raman spectra of free and adsorbed proteins reveals that the interaction apatite–protein happens through the carboxylate groups of the proteins. The combined analysis of CS, SSA and PS should be considered on the design of OHAp materials intended to interact with proteins. © 2013 Wiley Periodicals, Inc. J Biomed Mater Res Part A, 2013.