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Screening of Deconstructed Ion Channels with Venom Peptides

Abstract

Methods are shown to stabilise functional 8-15 kDa segments of acid sensing ion channels (ASICs) and voltage gated sodium channels (Na_Vs). The segments bind known venom peptides with nanomolar affinity, enabling high-throughput drug screening.

Short bio

Prof. Mehdi Mobli (BSc ChemEng, Chalmers, 2000, Sweden) received his PhD in physical organic chemistry from the University of Liverpool (UK) in 2004 through a collaborative project with GSK, focusing on the development of nuclear magnetic resonance (NMR) methods for automated characterisation of drug-like molecules. He undertook postdoctoral studies at the University of Connecticut Medical School (USA), the University of Manchester (UK), and the University of Queensland, where he notably contributed to the development of fast acquisition methods in multidimensional NMR spectroscopy and structural characterisation of venom peptides.