ISSN:2321-6212
Mostak Ahmed, Laura G Carrascosa, Paul Mainwaring and Matt Trau
University of Queensland, Australia
Posters & Accepted Abstracts: Res. Rev. J Mat. Sci
Protein phosphorylation is one of the most prominent post-translational mechanisms for protein regulation, which is frequently impaired in cancer. Through the covalent addition of phosphate groups to certain amino-acids, the interactions of former residues with nearby amino-acids are drastically altered, resulting in major changes of protein conformation that impacts its biological function. Herein, we report that these conformational changes can also disturb the protein�s ability to interact with and adsorb onto bare gold surfaces. Based on the direct interaction of proteins with the gold interface, we further developed an extremely simple method for aberrant phosphorylation detection that circumvents the current need for phospho-specific antibodies. The novel interfacial bio-sensing method, which only requires 50 ng of purified protein, was applied to EGFR phosphorylation analysis in several lung cancer cell lines and enabled monitoring their cell sensitivity to tyrosine kinase inhibitors (TKI) a drug frequently used in the clinic for lung cancer treatment.
E-mail:
m.ahmed2@uq.edu.au