A further insight into the adsorption mechanism of protein on hydroxyapatite by FTIR-ATR spectrometry

作者：Lin, Zhongyu^*; Hu, Ren; Zhou, Jianzhang; Ye, Yiwen; Xu, Zhaoxi; Lin, Changjian

来源：Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy , 2017, 173: 527-531.

DOI：10.1016/j.saa.2016.09.050

• BSA
• HA
• Protein adsorption
• Biomineralization
• FTIR-ATR
• IR spectroscopy

The adsorption mechanism of bovine serum albumin (BSA) on hydroxyapatite (HA) for different time intervals has been studied by Fourier transform infrared (FTIR)-attenuated total internal reflectance (ATR) spectrometry in this paper. The difference spectra obtained in HA and BSA frequency regions demonstrate that the binding of P=O, from the phosphate (PO43-) of HA, to the hydrogen of methyl (-CH3), methene (-CH2) and amideII (-CNH) in the protein appears to be much faster and stronger than that of the P-O group. In addition, Ca2+ must serve as a key role in the interaction of BSA with HA. The binding of Ca2+ to the oxygen of the peptide bond seems to induce a significant reconformation of polypeptide backbones from beta-pleated sheet to alpha-helix and beta-turn of helical circles. This alteration seems to have been accompanied by much hydrogen of polypeptides driven to bind PO43- and OH- of the HA actively and much -C = O and H-N- groups of the peptide bond freed from inter-chain hydrogen bonding to react on Ca2+ and combine strongly with the HA surface. This might be well expected to promote the HA biomineralization.

• 出版日期2017-2-15
• 单位厦门大学