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Sequencing of sulfonic acid derivatized peptides by electrospray mass spectrometry
Rapid Commun Mass Spectrom. 2000; 14(10):924-9.RC

Abstract

We report the application of nanoelectrospray ionization tandem mass spectrometry (nES-MS/MS) and capillary LC/microelectrospray MS/MS (cLC/&mgr;ES-MS/MS) for sequencing sulfonic acid derivatized tryptic peptides. These derivatives were specifically prepared to facilitate low-energy charge-site-initiated fragmentation of C-terminal arginine-containing peptides, and to enhance the selective detection of a single series of y-type fragment ions. Both singly and doubly protonated peptides were analyzed by MS/MS and the results were compared with those from their derivatized counterparts. Model peptides and peptides from tryptic digests of gel-isolated proteins were analyzed. Derivatized singly protonated peptides fragment in the same way by nES-MS/MS as they do by post-source decay matrix-assisted laser desorption/ionization mass spectrometry (PSD-MALDI-MS). They produce fragment ion spectra dominated by y-ions, and the simplified spectra are readily interpreted de novo. Doubly protonated peptides fragment in much the same way as their non-derivatized doubly protonated counterparts. The fragmentation of doubly protonated derivatives is especially useful for sequencing peptides that possess a proline residue near the N-terminus of the molecule. The singly protonated forms of these proline-containing derivatives often show enhanced fragmentation on the N-terminal side of the proline and considerably reduced fragmentation on the C-terminal side. In addition, sulfonic acid derivatization increases the in-source fragmentation of arginine-containing peptides. This could be useful for sequence verification and sequence tagging for use in single stage mass spectrometry. Copyright 2000 John Wiley & Sons, Ltd.

Authors+Show Affiliations

The Procter and Gamble Company, Miami Valley Laboratories, P.O. Box 538707, Cincinnati, OH 45253-8707, USA.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

10825258

Citation

Bauer, MD, et al. "Sequencing of Sulfonic Acid Derivatized Peptides By Electrospray Mass Spectrometry." Rapid Communications in Mass Spectrometry : RCM, vol. 14, no. 10, 2000, pp. 924-9.
Bauer MD, Sun Y, Keough T, et al. Sequencing of sulfonic acid derivatized peptides by electrospray mass spectrometry. Rapid Commun Mass Spectrom. 2000;14(10):924-9.
Bauer, M. D., Sun, Y., Keough, T., & Lacey, M. P. (2000). Sequencing of sulfonic acid derivatized peptides by electrospray mass spectrometry. Rapid Communications in Mass Spectrometry : RCM, 14(10), 924-9.
Bauer MD, et al. Sequencing of Sulfonic Acid Derivatized Peptides By Electrospray Mass Spectrometry. Rapid Commun Mass Spectrom. 2000;14(10):924-9. PubMed PMID: 10825258.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Sequencing of sulfonic acid derivatized peptides by electrospray mass spectrometry AU - Bauer,MD, AU - Sun,Y, AU - Keough,T, AU - Lacey,MP, PY - 2000/5/29/pubmed PY - 2000/5/29/medline PY - 2000/5/29/entrez SP - 924 EP - 9 JF - Rapid communications in mass spectrometry : RCM JO - Rapid Commun Mass Spectrom VL - 14 IS - 10 N2 - We report the application of nanoelectrospray ionization tandem mass spectrometry (nES-MS/MS) and capillary LC/microelectrospray MS/MS (cLC/&mgr;ES-MS/MS) for sequencing sulfonic acid derivatized tryptic peptides. These derivatives were specifically prepared to facilitate low-energy charge-site-initiated fragmentation of C-terminal arginine-containing peptides, and to enhance the selective detection of a single series of y-type fragment ions. Both singly and doubly protonated peptides were analyzed by MS/MS and the results were compared with those from their derivatized counterparts. Model peptides and peptides from tryptic digests of gel-isolated proteins were analyzed. Derivatized singly protonated peptides fragment in the same way by nES-MS/MS as they do by post-source decay matrix-assisted laser desorption/ionization mass spectrometry (PSD-MALDI-MS). They produce fragment ion spectra dominated by y-ions, and the simplified spectra are readily interpreted de novo. Doubly protonated peptides fragment in much the same way as their non-derivatized doubly protonated counterparts. The fragmentation of doubly protonated derivatives is especially useful for sequencing peptides that possess a proline residue near the N-terminus of the molecule. The singly protonated forms of these proline-containing derivatives often show enhanced fragmentation on the N-terminal side of the proline and considerably reduced fragmentation on the C-terminal side. In addition, sulfonic acid derivatization increases the in-source fragmentation of arginine-containing peptides. This could be useful for sequence verification and sequence tagging for use in single stage mass spectrometry. Copyright 2000 John Wiley & Sons, Ltd. SN - 1097-0231 UR - https://www.unboundmedicine.com/medline/citation/10825258/Sequencing_of_sulfonic_acid_derivatized_peptides_by_electrospray_mass_spectrometry L2 - https://doi.org/10.1002/(SICI)1097-0231(20000530)14:10<924::AID-RCM967>3.0.CO;2-X DB - PRIME DP - Unbound Medicine ER -
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