New Bioactive Composite Materials: Proteins Immobilized in the Layers of Alpha-Zr(IV) Phosphonates

9729178库马尔这项提议的目的是制定成功地将蛋白质固定在固体表面的战略。在本研究中，将制备具有特定功能的α-磷酸锆盐，并通过共价和非共价方法将选定的蛋白质固定在这些表面上。固定化蛋白质将通过漫反射光谱方法(紫外可见、傅里叶变换红外)、粉末X射线衍射、活性研究和差示扫描量热法进行检测。固定化蛋白的这些数据将与游离蛋白的数据进行比较，以深入了解表面功能、连接子长度和共价固定化如何影响结合蛋白的行为。这些详细的信息对于了解如何合理设计特定表面以最大限度地发挥结合蛋白的功能是必不可少的。由于酶的不稳定性和较高的成本，其催化效率和选择性没有被充分利用来满足社会需求。另一方面，固定化酶通常更稳定，成本更低，而且它们可以回收利用。固定化蛋白质在生物传感器、医用植入物、酶反应器和生物医学设备等领域具有重要的应用价值。固定化蛋白质可以提供新的和改进的催化剂来生产精细化学品、医药中间体和合成燃料，以满足日益增长的社会需求，同时减少人类活动对环境的影响。这项活动得到了化学司、材料研究司和战略规划局多学科活动办公室的共同支持。***

9729178 Kumar The aim of this proposal is to develop strategies for the successful immobilization of proteins at solid surfaces. In this study, a-zirconium phosphonates with specific functionalities will be prepared, and selected proteins will be immobilized at these surfaces by covalent and non-covalent methods. Immobilized proteins will be examined with diffuse reflectance spectral methods (Ultraviolet-Visible, Fourier Transform InfraRed), powder X-ray diffraction, activity studies, and by differential scanning calorimetry. These data for the immobilized proteins will be compared with those of the free proteins to gain insight into how surface functionalities, linker lengths, and covalent immobilization influence bound protein behavior. Such detailed information is essential to learn how specific surfaces can be rationally designed in order to maximize the bound protein function. %%% The catalytic efficiency and selectivity of enzymes have not been fully exploited for societal needs due to their instability and high cost. Immobilized enzymes, on the other hand, are often more stable, result in lower costs, and they can be recycled. Immobilized proteins are important for applications involving biosensors, medical implants, enzyme reactors, and biomedical devices. Immobilized proteins can provide new and improved catalysts to produce fine chemicals, pharmaceutical intermediates, and synthetic fuels to meet growing societal needs while reducing the environmental impact of human activities. This activity is jointly supported by the Division of Chemistry, the Division of Materials Research, and the Office of Multidisciplinary Activities in the MPS Directorate. ***