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Improved procedures for N-terminal sulfonation of peptides for matrix-assisted laser desorption/ionization post-source decay peptide sequencing.
Rapid Commun Mass Spectrom. 2004; 18(1):96-102.RC

Abstract

Post source decay (PSD) analysis of precursor ions generated from matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry is a powerful tool for amino acid sequencing and primary structure analysis of proteins. N-Terminal sulfonation has become an effective derivatization strategy in facilitating de novo peptide sequencing by the formation of predominate y-type ion series in MALDI PSD spectra. Recently, an effective and inexpensive N-terminal derivatization method has been reported using 4-sulfophenyl isothiocyanate (SPITC) as the derivatization reagent (J. Mass. Spectrom. 2003; 38: 373-377). In this paper, we report an improvement in the derivatization procedure with this reagent that involves replacing an organic co-reagent with other chemicals and eliminating the use of organic solvent. The method is demonstrated on a model peptide and on tryptic digests of two proteins. The results indicate that the improved sulfonation reaction can be implemented with high efficiency under aqueous conditions and that the sensitivity of mass detection can be increased considerably.

Authors+Show Affiliations

Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.No affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Evaluation Study
Journal Article
Research Support, U.S. Gov't, P.H.S.
Validation Study

Language

eng

PubMed ID

14689565

Citation

Wang, Dongxia, et al. "Improved Procedures for N-terminal Sulfonation of Peptides for Matrix-assisted Laser Desorption/ionization Post-source Decay Peptide Sequencing." Rapid Communications in Mass Spectrometry : RCM, vol. 18, no. 1, 2004, pp. 96-102.
Wang D, Kalb SR, Cotter RJ. Improved procedures for N-terminal sulfonation of peptides for matrix-assisted laser desorption/ionization post-source decay peptide sequencing. Rapid Commun Mass Spectrom. 2004;18(1):96-102.
Wang, D., Kalb, S. R., & Cotter, R. J. (2004). Improved procedures for N-terminal sulfonation of peptides for matrix-assisted laser desorption/ionization post-source decay peptide sequencing. Rapid Communications in Mass Spectrometry : RCM, 18(1), 96-102.
Wang D, Kalb SR, Cotter RJ. Improved Procedures for N-terminal Sulfonation of Peptides for Matrix-assisted Laser Desorption/ionization Post-source Decay Peptide Sequencing. Rapid Commun Mass Spectrom. 2004;18(1):96-102. PubMed PMID: 14689565.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Improved procedures for N-terminal sulfonation of peptides for matrix-assisted laser desorption/ionization post-source decay peptide sequencing. AU - Wang,Dongxia, AU - Kalb,Suzanne R, AU - Cotter,Robert J, PY - 2003/12/23/pubmed PY - 2004/3/25/medline PY - 2003/12/23/entrez SP - 96 EP - 102 JF - Rapid communications in mass spectrometry : RCM JO - Rapid Commun Mass Spectrom VL - 18 IS - 1 N2 - Post source decay (PSD) analysis of precursor ions generated from matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry is a powerful tool for amino acid sequencing and primary structure analysis of proteins. N-Terminal sulfonation has become an effective derivatization strategy in facilitating de novo peptide sequencing by the formation of predominate y-type ion series in MALDI PSD spectra. Recently, an effective and inexpensive N-terminal derivatization method has been reported using 4-sulfophenyl isothiocyanate (SPITC) as the derivatization reagent (J. Mass. Spectrom. 2003; 38: 373-377). In this paper, we report an improvement in the derivatization procedure with this reagent that involves replacing an organic co-reagent with other chemicals and eliminating the use of organic solvent. The method is demonstrated on a model peptide and on tryptic digests of two proteins. The results indicate that the improved sulfonation reaction can be implemented with high efficiency under aqueous conditions and that the sensitivity of mass detection can be increased considerably. SN - 0951-4198 UR - https://www.unboundmedicine.com/medline/citation/14689565/Improved_procedures_for_N_terminal_sulfonation_of_peptides_for_matrix_assisted_laser_desorption/ionization_post_source_decay_peptide_sequencing_ L2 - https://doi.org/10.1002/rcm.1289 DB - PRIME DP - Unbound Medicine ER -