摘要
以最终制备对人体安全无毒且补锌效果良好的类人胶原蛋白-锌螯合物为目标,利用紫外-可见吸收光谱法和荧光光谱法对类人胶原蛋白分子(HLC)与金属Zn(Ⅱ)离子之间的相互作用方式和机理进行了研究,其中Zn(Ⅱ)离子浓度为1.0×10-5—1.0×10-4mol/L;并通过荧光猝灭法计算出不同温度下(298 K和273 K)HLC分子与Zn(Ⅱ)离子之间的结合常数以及相应的热力学参数。研究结果表明:Zn(Ⅱ)离子对类人胶原蛋白的内源荧光有猝灭作用;根据Stern-Volmer方程的求解结果可知猝灭机制属于动态猝灭和静态猝灭;类人胶原蛋白分子和Zn(Ⅱ)离子以摩尔比1∶1形成胶原蛋白-锌螯合物;二者间的结合为自发反应,且相互作用力主要为疏水作用力。因此,文中的研究结果对类人胶原蛋白-Zn(Ⅱ)螯合物的工业化制备、理化性质探究以及进一步的应用研究提供了实验依据和理论基础。
In order to prepare the complex of human-like collagen （HLC） with zinc （Ⅱ） used as a zinc tonic, fluorescence spectroscopy and UV-VIS absorption spectroscopy were employed to analyze the binding mode and mechanism of Zn （Ⅱ） to human-like collagen, and fluorescence titration experiment was carried out with Zn （Ⅱ） concentrations from 1.0 10 -5 to 1.0 x 10 -4 mol/L at 298 K and 273 K to calculate the binding constants and the corresponding thermodynamic parameters. The experimental results indicate that Zn （I[） can quench the intrinsic fluorescence intensity of human- like collagen and the HLC-Zn（11） complex forms. According to the Stern-Volmer equation, the quenching mechanism belongs to both dynamic and static quenching during the binding process of zinc ions with protein molecules, and the number of binding points demonstrates that HLC and Zn （Ⅱ） form the complex of mole ratio 1：1. In addition, the binding process between the protein molecule and zinc（Ⅱ） ions is spontaneous and the hydrophobic interactions are the main binding force. The conclusion that Zn（Ⅱ） can bind to human-like collagen is clarified by all these experimental results and theoretical data, and it can be a useful guideline for the photodynamic process understanding, large-scale preparation and further application study of the HLC-Zn complex.
出处
《化学工程》
CAS
CSCD
北大核心
2013年第10期9-12,16,共5页
Chemical Engineering(China)
基金
陕西省教育厅自然科学专项项目(2013JK0703)
陕西省自然科学基础研究计划项目(2013JQ2025)
陕西学前师范学院科研基金项目(2013KJ082)
