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Analysis of the modification site in a small molecule-modified peptide by ion trap/time-of-flight hybrid mass spectrometry

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Abstract

Ion trap/time-of-flight hybrid mass spectrometers are powerful tools for the detailed structural analysis of modified peptides. We have analyzed Met-Lys-bradykinin modified with deoxycholate at the amino-terminus or the ε-amino group as model peptides. These two modified peptides produced fragment ions with the same nominal but different exact masses in tandem mass spectrometry with low-energy collision-induced dissociation. Accurate high-resolution analysis coupled with MS3 allowed us to distinguish the deoxycholate modification sites in the modified peptides.

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Abbreviations

CHCA:

α-Cyano-4-hydroxycinnamic acid

CID:

Collision-induced dissociation

DCA:

Deoxycholate

ESI:

Electrospray ionazation

HPLC:

High-performance liquid chromatography

MALDI:

Matrix-assisted laser desorpation ionization

MS:

Mass spectrometry

MS/MS:

Tandem mass spectrometry

TFA:

Trifluoroacetic acid

TOF:

Time-of-flight

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Acknowledgments

This work was supported in part by a grant from the Ministry of Education, Culture, Sports, Sciences, and Technology, and a grant-in-aid for cancer research from the Ministry of Health, Labor and Welfare of Japan.

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Correspondence to Junichi Goto.

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Mano, N., Kamota, M., Inohana, Y. et al. Analysis of the modification site in a small molecule-modified peptide by ion trap/time-of-flight hybrid mass spectrometry. Anal Bioanal Chem 386, 682–688 (2006). https://doi.org/10.1007/s00216-006-0696-7

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  • DOI: https://doi.org/10.1007/s00216-006-0696-7

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