Electrochemistry /Spectroscopy of Protein/Nanomaterial-B

导电聚合物已被用于修饰电极表面和固定化酶以构建 用于检测生物医学上重要物种的生物传感器，例如一氧化氮(NO)、葡萄糖、组胺、 我们将使用其他基质，如纳米材料，包括纳米管和纳米颗粒，硅溶胶， 表面活性剂和自组装单分子膜(SAM)用于修饰电极表面以实现固定化 以开发生物医学上重要物种的传感器，如NO、硫醇、组胺、 还有钙。在当前的授权期内，我们成功地测量了 肌红蛋白和细胞色素在用这些底物修饰的电极上的直接电化学。我们会 用这种方法来研究几种新的蛋白质，如Pirin、脱羧酶和Diheme 通过与密西西比大学医学中心的两名生物化学教授合作，研究蛋白质。 研究的假设如下：(1)用这些底物修饰的电极有助于携带 新蛋白质的直接电化学，以及(2)在这些底物上(或在这些底物中)保持的新蛋白质 天然形式或至少这些蛋白质没有变性。电化学方法，如循环 伏安法(CV)、差示脉冲伏安法(DPV)和方波伏安法(SWV)将用于 确定这些蛋白质在不同底物上(或在不同底物中)的形式电位。电化学也将是 用于探测金属中心(例如，Fe)与氧气、NO的相互作用以及相关的转录 辅因子P50等。这些研究将有助于找到蛋白质/基质系统，可能提供快速的 蛋白质分子与底物之间的电子转移速率对发展更加敏感 换能器。这些电化学研究也将为蛋白质化学提供有价值的信息。 参与生物医学研究。修饰电极上和溶液中的蛋白质分子 还将通过激光拉曼光谱、傅里叶变换红外光谱、紫外可见光谱、原子力等光谱方法对其进行表征 显微镜(AFM)、透射电子显微镜和扫描电子显微镜。这些研究将为相互作用提供光谱证据。 酶蛋白和修饰电极之间的差异，或许能够解释其中的差异。 蛋白质分子在不同底物上的电化学行为。

Conducting polymers have been used to modify electrode surfaces and to immobilize enzymes to construct biosensors for the detection of biomedically important species such as nitric oxide(NO), glucose, histamine, etc. We will use other substrates such as nanomaterials including nanotubes and nanoparticles, silica solgel, surfactants, and self-assembled monolayers (SAMs) to modify electrode surfaces for the immobilization of biomolecules in order to develop sensors for biomedically important species such as NO, thiols, histamine, and calcium. During the current grant period we have successfully measured the formal potentials of myoglobin and cytochromes by direct electrochemistry at electrodes modified with those substrates. We will use this approach to study several novel proteins such as pirin, decarboxylase enzymes, and diheme proteins by collaborating with two biochemistry professors at the University of Mississippi Medical Center. The hypotheses for the study are as follows:(1) the electrodes modified with those substrates help to carry out direct electrochemistry of novel proteins, and (2) the novel proteins on (or in) those substrates maintain the native form or at least these proteins are not denatured. Electrochemical methods such as cyclic voltammetry (CV), differential pulse voltammetry (DPV), and square wave voltammetry (SWV) will be used to determine the formal potentials of those proteins on (or in) different substrates. Electrochemistry will also be used to probe the interaction of the metal center (e.g., Fe) with dioxygen, NO, and the related transcriptional cofactors such as P50. These studies will help to find protein/matrix systems which may provide a fast electron transfer rate between the protein molecule and the substrate for the development of more sensitive transducers. These electrochemical studies will also provide valuable information for the protein chemistry involved in biomedical research. Those protein molecules on the modified electrodes as well as in solutions will also be characterized by spectroscopic methods including laser-Raman, FT-IR, UV-vis, atomic force microscopy (AFM), TEM, and SEM. These studies will provide spectroscopic evidence for the interactions between enzyme proteins and the modified electrodes and may be able to explain the differences.in electrochemical behaviors of protein molecules on different substrates.