Diagnostic protein discovery using liquid chromatography/mass spectrometry for proteolytic peptide targeting
Citations Over TimeTop 14% of 2005 papers
Abstract
A peptide targeting method has been developed for diagnostic protein discovery, which combines proteolytic digestion of fractionated plasma proteins and liquid chromatography coupled to electrospray time-of-flight mass spectrometry (LC/ESI-TOFMS) profiling. Proteolysis prior to profiling overcomes molecular weight limitations and compensates for the poor sensitivity of matrix-assisted laser desorption/ionization (MALDI) protein profiling. LC/MS increases the peak capacity compared to crude fractionation techniques or single sample MALDI analysis. Differentially expressed peptides are targeted in the mass chromatograms using bioinformatic techniques and subsequently sequenced with MALDI tandem MS. In a model study comparing pancreatic cancer patients to controls, 74% of the peptide targets were successfully sequenced. This profiling method was superior to previous experiments using single sample MALDI analysis for protein profiling or proteolytic peptide profiling, because more potential protein markers were identified.
Related Papers
- → Mass spectrometry and the age of the proteome(1998)724 cited
- → Applications of Tandem Mass Spectrometry (MS/MS) in Protein Analysis for Biomedical Research(2022)129 cited
- → Global internal standard technology for comparative proteomics(2002)184 cited
- → Labeling elastase digests with TMT: Informational gain by identification of poorly detectable peptides with MALDI‐TOF/TOF mass spectrometry(2010)23 cited
- → Mass spectrometry and the age of the proteome(1998)46 cited