ISSN: 0974-276X
Allan Stensballe
Denmark
Research Article
Optimizing the Identification of Citrullinated Peptides by Mass Spectrometry: Utilizing the Inability of Trypsin to Cleave after Citrullinated Amino Acids
Author(s): Tue Bennike, Kasper B. Lauridsen, Michael Kruse Olesen, Vibeke Andersen, Svend Birkelund and Allan StensballeTue Bennike, Kasper B. Lauridsen, Michael Kruse Olesen, Vibeke Andersen, Svend Birkelund and Allan Stensballe
Citrullinated proteins have been associated with several diseases and citrullination can most likely function as a target for novel diagnostic agents and unravel disease etiologies. The correct identification of citrullinated proteins is therefore of most importance. Mass spectrometry (MS) driven proteomics can with bottom up strategies analyze protein profiles and PTMs in complex samples. However, the site-specific characterization of citrullination using MS remains problematic, especially in complex samples where no sensitive chemical modification technique exists. A tryptic missed cleavage after citrulline is therefore often used as a marker for citrullination post processing. However, C-terminal tryptic citrullinated peptides have also been reported. In this study, we therefore aimed at optimizing the identification of citrullinated peptides in complex samples. To assess the cleav.. View More»
DOI:
10.4172/jpb.1000293