Mostak Ahmed, Laura G. Carrascosa*, Abu Ali Ibn Sina, Darren Korbie, Ke-lin Ru, Paul Mainwaring, and Matt Trau*

 

Centre for Personalized Nanomedicine, Australian Institute for Bioengineering and Nanotechnology (AIBN), The University of Queensland, Brisbane, QLD 4072, Australia

 

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 also enabled monitoring their cell sensitivity to tyrosine kinase inhibitors (TKI) ― a drug frequently used in the clinic for lung cancer treatment.


References: 
1Ahmed, M.; Carrascosa, L. G.; Sina, A. A. I.; Zarate, E. M.; Korbie, D.  Ru, K.-l.; Shiddiky, M. J.; Mainwaring, P.; Trau, M.; Biosens. Bioelectron. 2017, 91, 8-14. Detection of aberrant protein phosphorylation in cancer using direct gold-protein affinity interaction.


Biographic Details
Mr Mostak Ahmed
PhD candidate
Centre for Personalized Nanomedicine
AIBN, The University of Queensland, Australia
Phone: +61 414 633 302; E-mail: m.ahmed2@uq.edu.au
Research interests: Protein phosphorylation, Protein folding and misfolding, Electrochemistry