Tandem mass spectrometry investigation of ADP-ribosylated kemptide.
Tandem mass spectrometry investigation of ADP-ribosylated kemptide.
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DOI：
10.1016/j.jasms.2008.10.025
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发表时间：
2009-03
影响因子：
3.2
通讯作者：
Goodlett DR
中科院分区：
文献类型：
--
作者：
Hengel SM;Shaffer SA;Nunn BL;Goodlett DR
Bacterial ADP-ribosyltransferases (ADPRTs) are toxins that play a significant role in pathogenicity by inactivating host proteins through covalent addition of ADP-ribose. In this study we used ADP-ribosylated Kemptide as a standard to examine the effectiveness of three common tandem mass spectrometry fragmentation methods for assignment of amino acid sequence and site of modification. Fragmentation mechanisms investigated include low-energy collision induced dissociation (CID), infrared multiphoton dissociation (IRMPD), and electron capture dissociation (ECD); all were performed on a hybrid linear ion trap Fourier transform ion cyclotron resonance mass spectrometer. We show that ECD, but neither CID nor IRMPD, of ADP-ribosylated-Kemptide produces tandem mass spectra that are interpretable with regard to amino acid sequence assignment and site of modification. Examination of CID and IRMPD tandem mass spectra of ADP-ribosylated Kemptide revealed that fragmentation was primarily focused to the ADP-ribose region, generating several potential diagnostic ions for use in discovery of ADP-ribosylated proteins. Due to the lower relative sensitivity of ECD during data-dependent acquisition to CID, we suggest a two-fold strategy where CID and IRMPD are first used to detect ADP-ribosylated peptides, followed by sequence assignment and location of modification by ECD analysis.
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影响因子：
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通讯作者：
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