Department of Chemistry, National Dong Hwa University, Hualien 97403, Taiwan.
Medical Imaging Research Center, Institute for Radiological Research, Chang Gung University, Taoyuan 33302, Taiwan.
Int J Mol Sci. 2022 Jun 10;23(12):6521. doi: 10.3390/ijms23126521.
In the present study, molecularly imprinted polymers (MIPs) were used as a tool to grasp a targeted α-helix or β-sheet of protein. During the fabrication of the hinge-mediated MIPs, elegant cavities took shape in a special solvent on quartz crystal microbalance (QCM) chips. The cavities, which were complementary to the protein secondary structure, acted as a peptide conformational imprint (PCI) for adenylate kinase 1 (AK1). We established a promising strategy to examine the binding affinities of human AK1 in conformational dynamics using the peptide-imprinting method. Moreover, when bound to AK1, PCIs are able to gain stability and tend to maintain higher catalytic activities than free AK1. Such designed fixations not only act on hinges as accelerators; some are also inhibitors. One example of PCI inhibition of AK1 catalytic activity takes place when PCI integrates with an AK1 β-sheet. In addition, conformation ties, a general MIP method derived from random-coil AK1 in buffer/acetonitrile, are also inhibitors. The inhibition may be due to the need for this peptide to execute conformational transition during catalysis.
在本研究中，我们使用分子印迹聚合物（MIPs）作为工具来捕获蛋白质的靶向α-螺旋或β-折叠。在铰链介导的 MIPs 的制备过程中，在石英晶体微天平（QCM）芯片的特殊溶剂中形成了精致的腔。这些与蛋白质二级结构互补的腔充当了腺苷酸激酶 1（AK1）的肽构象印迹（PCI）。我们建立了一种有前途的策略，使用肽印迹法来研究人 AK1 在构象动力学中的结合亲和力。此外，当与 AK1 结合时，PCIs 能够获得稳定性，并倾向于保持比游离 AK1 更高的催化活性。这种设计的固定不仅在铰链上作为加速剂起作用;有些也是抑制剂。当 PCI 与 AK1 的β-折叠结合时，PCIs 抑制 AK1 催化活性就是一个例子。此外，构象键，一种源自缓冲液/乙腈中无规卷曲 AK1 的通用 MIP 方法，也是抑制剂。这种抑制可能是由于该肽在催化过程中需要执行构象转变。
