Using a Single Peptide to Electrochemically Sense Multiple Kinases

Ohad Solomon, Israel Alshanski, Ariel Shitrit, Yu Ju Chen, Assaf Friedler*, Shlomo Yitzchaik*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Kinases are responsible for regulating cellular and physiological processes, and abnormal kinase activity is associated with various diseases. Therefore, kinases are being used as biomarkers for disease and developing methods for their sensing is highly important. Usually more than one kinase is involved in phosphorylating a target protein. However, kinase detection methods usually detect the activity of only one specific kinase. Here we describe an electrochemical kinase sensing tool for the selective detection of two kinases using the same target peptide. We demonstrate the sensing of kinases ERK2 and PKCδ. This is based on a single sensing element, a peptide that contains two distinct phosphorylation sites of these two kinases. Reversibility experiments with alkaline phosphatase and reaction with the electrochemically active ferrocene-labeled ATP showed that the mechanism of sensing is by detecting the enzymatic phosphorylation. Our approach can be further utilized to develop devices for the detection of multiple kinases and can be expanded to other types of enzymes involved in disease.

Original languageAmerican English
Pages (from-to)351-357
Number of pages7
JournalBiochemistry
Volume62
Issue number2
DOIs
StatePublished - 17 Jan 2023

Bibliographical note

Publisher Copyright:
© 2022 American Chemical Society.

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