中文摘要：

采用傅里叶变换红外衰减全反射（FTIR-ATR）光谱法对牛血清白蛋白（BSA）在羟磷灰石（HA）[Ca（10）（OH）2（PO4）6]表面不同时间的相互吸附作用进行了表征。在BSA溶液作用下,羟磷灰石表面的Ca2＋、PO43-和OH-离子初始的溶解和再沉淀使得BSA与HA相互作用层层叠加,在HA表面形成从表层到次表层分子都包含有吸附的BSA的覆盖层,从而加深两者之间的相互作用。经红外差谱法处理过的相关ATR数据表明,BSA与HA之间的相互作用是快速的,并随时间变化进一步加强;来自HA上PO4^3-的P=O基团对蛋白质肽键的酰胺Ⅱ带（-CNH）、多肽链的甲基（-CH3）和亚甲基（-CH2）上氢的吸附作用要比P-O快速而且强烈。Ca2＋在该吸附过程中起了极其重要的作用,其快速与蛋白质肽键的羰基氧发生作用,并诱导该蛋白质二级结构由β-折叠向α-螺旋和β-转角构象转变;伴随着这一构象变化,蛋白质多肽链上大多数肽键的-C=O和H-N-活性基团从链间氢键交联中释放出来,带动众多的氢分别参与同HA表面的Ca2＋、PO43-和OH-离子的相互吸附作用,并牢牢地结合于HA表面;这对硬组织的再生起着重要作用,促进了HA的生物矿化过程。

英文摘要：

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 PO43-,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 Ca~（2＋） plays an important role in the interaction of BSA with HA.It appears that the binding of Ca~（2＋） to the carbonyl-oxygen of the peptide bond in BSA caused 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 OH~-effectively and much-C=O and H-N- groups of the peptide bond being freed from inter-chain hydrogenbonding to act on Ca~（2＋） 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 Ca~（2＋） 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.