Project Summary

Protein phosphorylation is one of the most prominent post-translational modifications for protein regulation. This ubiquitous mechanism, however, is susceptible to alteration by the emergence and progression of cancer. Covalent addition of phosphate groups to certain amino-acids, and the interactions of former residues with nearby amino-acids become drastically altered, resulting in major protein conformation changes that impact its biological function. Serendipitously, these conformational changes can also disturb the protein's ability to interact with and adsorb onto bare gold surfaces (flat or nanoparticles). Based on this measurable change in the interaction of proteins with the bare gold interface, we are now developing simple, yet accurate, electrochemical and colorimetric tests that can detect the presence of cancer and chart its growth.

This project will provide an opportunity for students to acquire skills in molecular biology, biochemistry and electrochemistry.

Research Group

Trau Group

Keywords

Protein phosphorylation, Protein conformation, Protein-Gold affinity, Electrochemistry, Colorimetry

An example of the workflow of label free electrochemical detection of protein phosphorylation using protein-bare flat gold interaction (For details, see M. Ahmed et al., Biosens. Bioelectron., 91, 8 (2017).)

 

Project members

Lead Investigator

Professor Matt Trau

Senior Group Leader
Trau Group