Citation: YE Qing, HU Ren, ZHOU Jian-Zhang, YE Yi-Wen, XU Zhao-Xi, LIN Chang-Jian, LIN Zhong-Yu. FTIR-ATR Spectrometry of BSA Adsorption on Hydroxyapatite[J]. Acta Physico-Chimica Sinica, ;2016, 32(2): 565-572. doi: 10.3866/PKU.WHXB201511301 shu

FTIR-ATR Spectrometry of BSA Adsorption on Hydroxyapatite

1.
1 State Key Laboratory of Physical Chemistry of Solid Surfaces, Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, Fujian Province, P. R. China;
2.
2 Chuyang Honors College, Zhejiang Normal University, Jinhua 321004, Zhejiang Province, P. R. China;
3.
3 Xiamen AERTE System Engineering CO., LTD, Xiamen 361005, Fujian Province, P. R. China

Corresponding author: LIN Zhong-Yu,
Received Date: 2 July 2015
Available Online: 26 November 2015
Fund Project: 国家自然科学基金(51571169)资助项目 (51571169)

The microcosmic process of bovine serum albumin (BSA) adsorbing onto hydroxyapatite (HA) for different time intervals was investigated by Fourier transform infrared attenuated total internal reflectance (FTIRATR) spectrometry. The initial dissolution and re-precipitation of PO₄^3-, Ca²⁺, and OH^- ions from the HA coating led to the occurrence of the coating including adsorbed BSA on the HA from surface-to subsurface-molecular layers and to in-depth interaction between BSA and HA. The subtraction results gained in the adsorption regions of HA and BSA reveal that the binding of P=O, from the phosphate (PO₄^3-), to the hydrogen of amide II, methyl and methene of the BSA appears to be considerably more rapid and stronger than that of the P―O group. In addition, it is very likely that Ca²⁺ plays an important role in the interaction of BSA with HA. It appears that the binding of Ca²⁺ to the carbonyl-oxygen of the peptide bond in BSAcaused a significant, molecular, conformational rearrangement of polypeptide backbones from β-pleated sheet to helical circles of α-helix and β-turn. This change appears to have been followed by much hydrogen of polypeptides being driven to bind PO₄^3- and OHeffectively and much ―C=O and H―N―groups of the peptide bond being freed from inter-chain hydrogenbonding to act on Ca²⁺ and combine strongly with the HA surface. This might reasonably be expected to promote hard tissue regeneration. BSA seems to be activated by the inductive effect of Ca²⁺ via the molecular rearrangement of polypeptide backbones from pleated sheet to helical circles and in turn reacts strongly on the HA, resulting in profound effects on the course of biomineralization.
- Biomaterial,
- Protein adsorption,
- Polypeptide,
- IR spectroscopy,
- FTIR-ATR,
- Biomineralization
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