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作 者:贾二娜 林园[1] 苏朝晖[1,2] JIA Er-Na;LIN Yuan;SU Zhao-Hui(State Key Laboratory of Polymer Physics and Chemistry,Changchun Institute of Applied Chemistry,Chinese Academy of Sciences,Changchun 130022,China;University of Science and Technology of China,Hefei 230026,China)
机构地区:[1]中国科学院长春应用化学研究所,长春130022 [2]中国科学技术大学,合肥230026
出 处:《分析化学》2021年第1期121-127,共7页Chinese Journal of Analytical Chemistry
基 金:国家自然科学基金项目(No.21429401);国家公派留学基金项目(No.201904910172)资助。
摘 要:血液中的蛋白质在接触材料表面的吸附行为与方式是影响植入材料血液相容性的重要因素。本研究利用硅烷偶联剂在二氧化钛纳米管基底上制备了富含氨基与羧基的表面,并通过共价偶联的方式,将牛血清白蛋白(BSA)与纤维蛋白原(Fib)固定到二氧化钛纳米管表面。通过对蛋白质吸附及表面血小板粘附行为的研究探讨了BSA与Fib的二级结构变化与血小板粘附行为之间的关系。研究发现,经羧基固定的BSA和氨基固定的Fib表面蛋白质二级结构中的β-折叠和β-转角比例较高,血液相容性更好;同时BSA对血小板的粘附具有选择性,当采用氨基固定BSA时,会导致识别血小板中的特异性受体序列暴露,血小板激活程度增加。The adsorption behavior of proteins in blood on the surface of the contact material is an important factor affecting the blood compatibility of the implanted material.In order to establish the relationship between protein conformation and blood compatibility,the surfaces of amino and carboxyl groups on the titanium dioxide nanotubes were fabricated by grafting silane coupling agent,and bovine serum albumin(BSA)and fibrinogen(Fib)were fixed to the surface through EDC/NHS chemical crosslinking.The relationship between the secondary structure changes of BSA and Fib and platelet adhesion behavior was investigated by studying protein adsorption and surface platelet adhesion behavior.The results showed that the ratios ofβ-sheet toβ-turn in the secondary structure of proteins on the surface of carboxyl immobilized-BSA and amino immobilized Fib were higher,and the blood compatibility was better.Furthermore,BSA adhesion to platelets was selective,the amino-binding protein led to exposure of specific receptors that recognize platelets,and platelet activation increased.
关 键 词:二氧化钛纳米管 蛋白质吸附 构象变化 血小板粘附
分 类 号:R318.08[医药卫生—生物医学工程]
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