Novel Method for Identification of Protein Arginine-ADP-ribosylation Based on Chemical Derivatization and CID Fragmentation

doi:10.7503/cjcu20130824

Abstract

Abstract:

High performance liquid chromatography coupled to electrospray ionization mass spectrometry(MS) was widely used to map protein posttranslational modifications in complex biological samples. But frequently-used collision induced dissociation(CID) was unsuccessful in fragmentizing arginine adenosine diphosphate(ADP)-ribosylated peptides because the spectra from CID fragmentation were dominated by ADP-ribose fragment ions at the expense of the fragments generated from peptide backbone, making the assignment of the peptide sequence very difficult. In this work, a novel method was developed for identification of arginine ADP-ribosylated peptides based on CID fragmentation. Arginine ADP-ribosylated angiotensin-Ⅰ was either converted to ornithinylated angiotensin-Ⅰ under alkaline condition or hydrolyzed to arginine ribosylated angiotensin-Ⅰ by treatment with phosphodiesterase and alkaline phosphatase. The two derivatives were then subjected to CID fragmentation during tandem MS analysis. Compared with unmodified ADP-ribosylated angiotensin-Ⅰ, the two derivatives generated more sequence specific ions in the spectra, giving enough information to localize the site of arginine ADP-ribosylation.

Key words: Angiotensin-Ⅰ, Chemical derivatization, Collision induced dissociation, Mass spectrometry, Arginine adenosine diphosphate(ADP)-ribosylation

CLC Number:

O657.63

TrendMD:

ZHAO Zhi-Qiang, QIU Hui-Hua, YAO Jun, CHEN Yong-Feng. Novel Method for Identification of Protein Arginine-ADP-ribosylation Based on Chemical Derivatization and CID Fragmentation[J]. Chem. J. Chinese Universities, 2013, 34(12): 2704.

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