PeptideTracker: A knowledgebase for collecting and storing information on protein concentrations in biological tissues

Targeted proteomics using multiple reaction monitoring (MRM) has become the method of choice for the rapid, precise, and reproducible quantitation of proteins in complex biological matrices. MRM-based targeted proteomics allows protein profiling in complex biological samples and accurate comparisons of between samples [1-6], typically using a bottom-up LC-MS/MS approach [7]. While relative quantitation approaches report differences in fold-changes between the samples being compared, absolute methods measure the concentrations [8], ideally based on isotopically labeled internal standard peptides that are analogues of the endogenous proteotypic target peptides [9]. The use of stable-isotope labeled standard (SIS) peptides is a key factor in the precision and reproducibility of absolute quantitation experiments using LC/MRM-MS, but the results may still not be accurate. Experimentally derived concentrations for specific tissues or biofluids can vary as a function of digestion protocol, or even which peptides are selected to represent a given protein [10-12].This article is protected by copyright. All rights reserved