Atomic force microscopy characterization of kinase-mediated phosphorylation of a peptide monolayer

Roman Zhuravel, Einav Amit, Shir Elbaz, Dvir Rotem, Yu Ju Chen, Assaf Friedler, Shlomo Yitzchaik*, Danny Porath

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

We describe the detailed microscopic changes in a peptide monolayer following kinase-mediated phosphorylation. A reversible electrochemical transformation was observed using square wave voltammetry (SWV) in the reversible cycle of peptide phosphorylation by ERK2 followed by dephosphorylation by alkaline phosphatase. A newly developed method for analyzing local roughness, measured by atomic force microscope (AFM), showed a bimodal distribution. This may indicate either a hole-formation mechanism and/or regions on the surface in which the peptide changed its conformation upon phosphorylation, resulting in increased roughness and current. Our results provide the mechanistic basis for developing biosensors for detecting kinase-mediated phosphorylation in disease.

Original languageAmerican English
Article number36793
JournalScientific Reports
Volume6
DOIs
StatePublished - 14 Nov 2016

Bibliographical note

Publisher Copyright:
© The Author(s) 2016.

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