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BSA与羟磷灰石相互吸附的FTIR-ATR光谱

叶青 ,  胡仁 ,  周剑章 ,  叶艺文 ,  许朝曦 ,  林昌健 ,  林种玉

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引用本文: 叶青, 胡仁, 周剑章, 叶艺文, 许朝曦, 林昌健, 林种玉. BSA与羟磷灰石相互吸附的FTIR-ATR光谱[J]. 物理化学学报, 2016, 32(2): 565-572. doi: 10.3866/PKU.WHXB201511301 shu
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

BSA与羟磷灰石相互吸附的FTIR-ATR光谱

  • 1.

    1 厦门大学化学化工学院化学系, 固体表面物理化学国家重点实验室, 福建厦门 361005;

  • 2.

    2 浙江师范大学初阳学院, 浙江金华 321004;

  • 3.

    3 厦门阿尔特系统工程有限公司, 福建厦门 361005

    • 通讯作者: 林种玉
  • 基金项目:

    国家自然科学基金(51571169)资助项目 (51571169)

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)[Ca10(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PO43-的P=O基团对蛋白质肽键的酰胺II 带(―CNH)、多肽链的甲基(―PO3)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。

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