17th International Mass Spectrometry Conference :: Prague, 2006
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|Presentation date:||Tue, Aug 29, 2006|
|Presentation time:||14:30 – 16:00|
Christopher John Arthur1, Alex Stuart1, Laura Rigau-Roca1, Mathew Phillip Crump1, John Crosby1 University of Bristol, Bristol, United Kingdom
Correspondence address: Christopher J. Arthur, University of Bristol, School of Chemistry, Cantock's Close, Bristol, BS8 1TS United Kingdom.
Keywords: Automation; Complex, Non-Covalent; Experimental Design; Protein.
Novel aspect: Optimisation of sample preparation and analysis for study of biomolecular complexes.
The utility of mass spectrometry for the rapid automated screening of protein small molecule ligands is of considerable interest both academically and to the pharmaceutical industry. A number of problems prevent its general utility. Reproducibility issues both between samples and sources and the effects of the potential ligand mixtures utilised on sample ionisation can have significant and deleterious effects on the automated or semi-automated screening of libraries of compounds.
In this poster we present a strategy for the robust optimisation of native mass spectrometry for screening applications. By using a mixture of factorial and Taguchi experimental design methods buffer components, source conditions and analyser conditions may be optimised thus permitting the reproducible and robust analysis of protein-ligand interactions. We demonstrate this strategy for the optimisation of a variety of model systems. Furthermore, the utility of the Advion Nanomate™ for the automated screening of compounds against a medicinally relevant target will be discussed.