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

这一建议的目的是制定策略，成功地固定在固体表面的蛋白质。在本研究中，将制备具有特定功能的磷酸锆，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。固定化蛋白质将通过漫反射光谱方法（紫外可见，傅立叶变换红外），粉末x射线衍射，活性研究和差示扫描量热法进行检查。这些固定蛋白的数据将与自由蛋白的数据进行比较，以深入了解表面功能、连接体长度和共价固定如何影响结合蛋白的行为。这些详细信息对于了解如何合理设计特定表面以最大化结合蛋白的功能至关重要。酶的催化效率和选择性由于其不稳定性和高成本尚未充分开发用于社会需要。另一方面，固定化酶通常更稳定，成本更低，而且可以回收利用。固定化蛋白对于生物传感器、医疗植入物、酶反应器和生物医学设备的应用非常重要。固定化蛋白质可以为生产精细化学品、医药中间体和合成燃料提供新的和改进的催化剂，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。这项活动由化学司、材料研究司和公安部多学科活动办公室共同支持。＊＊＊

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. ***