School of Mechanical Engineering, Qinghai University, Xining 810016, China.
Research Center of Basic Medical Science, Medical College, Qinghai University, Xining 810016, China.
Biosensors (Basel). 2022 Oct 12;12(10):865. doi: 10.3390/bios12100865.
Abnormal protein phosphorylation may relate to diseases such as Alzheimer's, schizophrenia, and Parkinson's. Therefore, the real-time detection of phosphoproteins in sweat was of great significance for the early knowledge, detection, and treatment of neurological diseases. In this work, anatase/rutile TiO was in situ grown on the MXene surface to constructing the intercalation structure MXene@anatase/rutile TiO ternary heterostructure as a sensing platform for detecting phosphoprotein in sweat. Here, the intercalation structure of MXene acted as electron and diffusion channels for phosphoproteins. The in situ grown anatase/rutile TiO with n-n-type heterostructure provided specific adsorption sites for the phosphoproteins. The determination of phosphoprotein covered concentrations in sweat, with linear range from 0.01 to 1 mg/mL, along with a low LOD of 1.52 μM. It is worth noting that, since the macromolecular phosphoprotein was adsorbed on the surface of the material, the electrochemical signal gradually decreased with the increase of phosphoprotein concentration. In addition, the active sites in the MXene@anatase/rutile TiO ternary heterojunction and synergistic effect of the heterojunction were verified by first-principle calculations to further realize the response to phosphoproteins. Additionally, the effective diffusion capacity and mobility of phosphoprotein molecules in the ternary heterojunction structure were studied by molecular dynamics simulation. Furthermore, the constructed sensing platform showed high selectivity, repeatability, reproducibility, and stability, and this newly developed sensor can detect for phosphoprotein in actual sweat samples. This satisfactory sensing strategy could be promoted to realize the noninvasive and continuous detection of sweat.
异常的蛋白质磷酸化可能与阿尔茨海默病、精神分裂症和帕金森病等疾病有关。因此,实时检测汗中的磷酸化蛋白对于早期认识、检测和治疗神经疾病具有重要意义。在这项工作中,锐钛矿/rutileTiO2 被原位生长在 MXene 表面,构建了夹层结构 MXene@anatase/rutileTiO2 三元异质结构作为检测汗中磷酸化蛋白的传感平台。在这里,MXene 的夹层结构作为电子和扩散通道,用于磷酸化蛋白。具有 n-n 型异质结构的原位生长的锐钛矿/rutileTiO2 为磷酸化蛋白提供了特定的吸附位点。在汗中检测磷酸化蛋白的浓度范围为 0.01 至 1mg/mL,具有低至 1.52μM 的 LOD。值得注意的是,由于大分子磷酸化蛋白被吸附在材料表面,随着磷酸化蛋白浓度的增加,电化学信号逐渐降低。此外,通过第一性原理计算进一步验证了 MXene@anatase/rutileTiO2 三元异质结中的活性位点和异质结的协同作用,以进一步实现对磷酸化蛋白的响应。此外,通过分子动力学模拟研究了三元异质结结构中磷酸化蛋白分子的有效扩散能力和迁移率。此外,所构建的传感平台表现出高选择性、重复性、重现性和稳定性,并且这种新开发的传感器可以检测实际汗样中的磷酸化蛋白。这种令人满意的传感策略可以促进实现对汗液的非侵入性和连续检测。