State Key Laboratory of Physical Chemistry of Solid Surfaces and Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, PR China.
State Key Laboratory of Physical Chemistry of Solid Surfaces and Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, PR China.
Spectrochim Acta A Mol Biomol Spectrosc. 2017 Feb 15;173:527-531. doi: 10.1016/j.saa.2016.09.050. Epub 2016 Sep 30.
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 PO, from the phosphate (PO) of HA, to the hydrogen of methyl (-CH), methene (-CH) and amideII (-CNH) in the protein appears to be much faster and stronger than that of the PO group. In addition, Ca must serve as a key role in the interaction of BSA with HA. The binding of Ca to the oxygen of the peptide bond seems to induce a significant reconformation of polypeptide backbones from β-pleated sheet to α-helix and β-turn of helical circles. This alteration seems to have been accompanied by much hydrogen of polypeptides driven to bind PO and OH of the HA actively and much -C=O and HN groups of the peptide bond freed from inter-chain hydrogen bonding to react on Ca and combine strongly with the HA surface. This might be well expected to promote the HA biomineralization.
本文通过傅里叶变换衰减全内反射红外光谱（FTIR-ATR）研究了牛血清白蛋白（BSA）在不同时间间隔内在羟基磷灰石（HA）上的吸附机制。在 HA 和 BSA 频率区域获得的差谱表明，来自 HA 的磷酸盐（PO）的 PO 与蛋白质中甲基（-CH）、亚甲基（-CH2）和酰胺 II（-CNH）的氢之间的结合似乎比 PO 基团快得多且强得多。此外，Ca 似乎在 BSA 与 HA 的相互作用中起关键作用。Ca 与肽键氧的结合似乎诱导多肽主链从β-折叠片层到α-螺旋和螺旋圈的β-转角的显著重排。这种变化似乎伴随着多肽的许多氢被驱动，积极地与 HA 的 PO 和 OH 结合，肽键的许多-C=O 和 HN 基团从链间氢键中释放出来，与 Ca 反应并与 HA 表面强烈结合。这很可能有助于促进 HA 的生物矿化。
