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High protein adsorptive capacity of amino acid‐functionalized hydroxyapatite
Author(s) -
Lee WingHin,
Loo ChingYee,
Zavgorodniy Alexander V.,
Rohanizadeh Ramin
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.34383
Subject(s) - lysozyme , protein adsorption , adsorption , crystallinity , amino acid , materials science , macromolecule , precipitation , surface modification , chemical engineering , polymer chemistry , nuclear chemistry , biochemistry , chemistry , organic chemistry , composite material , physics , meteorology , engineering
Charged functional groups present on the surface of biomaterials play an important role to regulate the affinity and attachment of macromolecules, including proteins, on the surface of biomaterials. In this study, the protein adsorptive capacity of hydroxyapatite (HA) was regulated by introducing different amino acids during the precipitation of HA. After incubation of HA samples in 5000 μg/mL lysozyme solution at pH 7.4 for 24 h, unmodified HA adsorbed 0.886 mg/m 2 of lysozyme while amino acid‐functionalized HA (AA‐HA) particles demonstrated higher adsorption capacity ranging from 1.090 to 1.680 mg/m 2 . Incorporation of amino acids with longer side chain lengths decreased the crystallinity and increased the negative value of the surface charge of HA particles. The specific surface areas were significantly increased in the presence of amino acids. Protein loading capacity onto AA‐HA was further enhanced by regulating the pH of working solution whereby the protein adsorption rate increased with decreasing the pH, while reverse trend obtained in unmodified HA. The study demonstrated that the amount of adsorbed lysozyme onto AA‐HA particles was correlated with the particles' surface charges. © 2012 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 101A: 873–883, 2013.