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Probing of Protein Kinase Activity by Electrochemistry

机译:通过电化学探测蛋白激酶活性

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Protein kinase can catalyze the transfer of a phosphoryl group from adenosine triphosphate (ATP) toprotein/peptide substrate at the serine, tyrosine or threonine residues. The phosphorylation can inducethe surface charge change of substrate peptides-modified electrode; the reaction could be measured bythe change of the electrochemical impedance or the tyrosine oxidation current. The phosphate groupscan be selectively recognized by anti-phosphorylated peptide antibody and metal ions, metalcomplexes as well as metal nanoparticles through the coordination or electrostatic interaction, whichfacilitated the design of various electrochemical kinase biosensors. Furthermore, the phosphate- modified ATP analogues (e.g. biotinylated, sulfated and ferrocene-labeled ATP) have been used as theco-substrates of phosphorylation to monitor protein kinase activity. All of these electrochemicalstrategies for kinase assays were summarized in the present work.
机译:蛋白激酶可以催化磷酸基团从三磷酸腺苷(ATP)到丝氨酸,酪氨酸或苏氨酸残基的蛋白质/肽底物的转移。磷酸化可以诱导底物肽修饰电极的表面电荷变化。反应可以通过电化学阻抗或酪氨酸氧化电流的变化来测量。磷酸基团可以通过配位或静电相互作用被抗磷酸化的肽抗体和金属离子,金属配合物以及金属纳米颗粒选择性地识别,这有助于设计各种电化学激酶生物传感器。此外,磷酸修饰的ATP类似物(例如生物素化的,硫酸化的和二茂铁标记的ATP)已被用作磷酸化的共底物以监测蛋白激酶活性。在目前的工作中总结了用于激酶测定的所有这些电化学策略。

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