Conformational Changes of Fibrinogen Adsorption onto Hydroxyapatite and Titanium Oxide Nanoparticles.
Conformational Changes of Fibrinogen Adsorption onto Hydroxyapatite and Titanium Oxide Nanoparticles.
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DOI：
10.1006/jcis.1999.6159
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发表时间：
1999-06
影响因子：
9.9
通讯作者：
Yongli;Xiu-fang;Yandao;Nanming;Tingying;Xinqi
中科院分区：
文献类型：
--
作者：
Yongli;Xiu-fang;Yandao;Nanming;Tingying;Xinqi
表面吸附对蛋白质结构的影响在生物、医学和工业领域受到越来越多的关注。用差示扫描量热法(DSC)、圆二色谱(CD)和荧光光谱研究了纤维蛋白原在二氧化钛和透明质酸上的吸附结构。结果表明，二氧化钛表面使蛋白质的有序二级结构略有减少，纤维蛋白原的构象进一步发生了洗涤和脱附。在吸附、洗涤和解吸过程中，α-螺旋含量逐渐减少。结果还被用来估计蛋白质在吸附和解吸状态下的整体结构。值得注意的是，在每种情况下，纤维蛋白原在HA上的吸附转变热都有所增加。在被测试的三种情况中，有两种情况下吸附在二氧化钛上时，转变热增加。结合不同离子强度下纤维蛋白原的DSC热图，表明静电作用是控制纤维蛋白原在二氧化钛和透明质酸上吸附的主要机制。版权所有1999年学术出版社。
The effect of surface adsorption on protein structure is of increasing interest in the biological, medical, and industrial fields. The structure of fibrinogen, a major plasma protein, adsorbed onto TiO2 and HA was examined by employing differential scanning calorimetry (DSC), circular dichroism (CD), and fluorescence spectroscopy. It was found that the TiO2 surface slightly decreased the ordered secondary structure of the protein; the fibrinogen conformation further changed upo washing and desorption. The alpha-helix content decreased gradually during the adsorption, washing, and desorption processes. The results were also used to estimate the overall structure of the protein in the adsorbed and desorbed states. It is significant that the fibrinogen transition enthalpy increased in each case upon adsorption onto HA. The transition enthalpy increased upon adsorption onto TiO2 in two out of three cases tested. These results, combined with the DSC thermograms of fibrinogen at different ionic strengths, suggest that electrostatic interactions are the main mechanism controlling the adsorption of fibrinogen to TiO2 and HA. Copyright 1999 Academic Press.