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Isotope-differentiated binding energy shift tags (IDBEST™)
Poster Presented at the 53rd Annual ASMS Conference June 6-9, 2005, San Antonio, TX.
Abstract
Luke V. Schneider, Michael P. Hall, John P. Wilson, Lane A. Clizbe, and Siamak Ashrafi
Current global proteomic methods have too limited a dynamic range (hence sensitivity) and resolution to adequately identify low abundance biomarkers in human tissues. High abundance protein depletion and subcellular fractionation methods can extend global analyses a few orders of magnitude, but still fall short of measuring the known abundance levels of the majority of proven clinical biomarkers. More importantly, global (hypothesis-free) MS proteomics methods (e.g. ICAT™, GIST, iTRAQ™, and iPROT™) are time and cost-intensive because the peptide complexity must be reduced prior to MS analysis. The selective enrichment of Cys- or His-containing peptides also significantly reduces sequence coverage, inhibiting the identification of protein variants (isoforms). Isoforms are increasingly important in disease diagnostics, staging, drug efficiency, and drug toxicity. Without the benefit of the molecular-level detail uniquely provided by MS, ELISA and protein chip assays also fail to identify unknown protein variants and can be confounded by crossreactive protein species.
IDBEST™ is a cost-effective tool for hypothesis-driven biomarker discovery, validation, and screening. The technology allows a mass spectrometer to be used as a quantitative detector for protein microarray experiments for the first time. IDBEST™ assays can enrich low abundance biomarkers that are lost in global proteomic analysis techniques due to competitive ionization issues in the mass spectrometer.
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