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Atmospheric pressure matrix-assisted laser desorption/ionization ion trap mass spectrometry of sulfonic acid derivatized tryptic peptides.
Rapid Commun Mass Spectrom. 2001; 15(23):2227-39.RC

Abstract

Atmospheric pressure matrix-assisted laser desorption/ionization (AP-MALDI) and ion trap mass spectrometry have been used to study the fragmentation behavior of native peptides and peptide derivatives prepared for de novo sequencing applications. Sulfonic acid derivatized peptides were observed to fragment more extensively and up to 28 times more efficiently than the corresponding native peptides. Tandem mass spectra of native peptides containing aspartic or glutamic acids are dominated by cleavage on the C-terminal side of the acidic residues. This significantly limits the amount of sequence information that can be derived from those compounds. The MS/MS spectra of native tryptic peptides containing oxidized Met residues show extensive loss of CH(3)SOH and little sequence-specific fragmentation. On the other hand, the tandem mass spectra of derivatized peptides containing Asp, Glu and oxidized Met show much more uniform fragmentation along the peptide backbone. The AP-MALDI tandem mass spectra of some derivatized peptides were shown to be qualitatively very similar to the corresponding vacuum MALDI postsource decay mass spectra, which were obtained on a reflector time-of-flight instrument. However, the ion trap mass spectrometer offers several advantages for peptide sequencing relative to current reflector time-of-flight instruments including improved product ion mass measurement accuracy, improved precursor ion selection and MS(n). These latter capabilities were demonstrated with solution digests of model proteins and with in-gel digests of 2D-gel separated proteins.

Authors+Show Affiliations

The Procter and Gamble Company, Miami Valley Laboratories, PO Box 538707, Cincinnati, OH 45253-8707, USA. keough.tw@pg.comNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

11746890

Citation

Keough, T, et al. "Atmospheric Pressure Matrix-assisted Laser Desorption/ionization Ion Trap Mass Spectrometry of Sulfonic Acid Derivatized Tryptic Peptides." Rapid Communications in Mass Spectrometry : RCM, vol. 15, no. 23, 2001, pp. 2227-39.
Keough T, Lacey MP, Strife RJ. Atmospheric pressure matrix-assisted laser desorption/ionization ion trap mass spectrometry of sulfonic acid derivatized tryptic peptides. Rapid Commun Mass Spectrom. 2001;15(23):2227-39.
Keough, T., Lacey, M. P., & Strife, R. J. (2001). Atmospheric pressure matrix-assisted laser desorption/ionization ion trap mass spectrometry of sulfonic acid derivatized tryptic peptides. Rapid Communications in Mass Spectrometry : RCM, 15(23), 2227-39.
Keough T, Lacey MP, Strife RJ. Atmospheric Pressure Matrix-assisted Laser Desorption/ionization Ion Trap Mass Spectrometry of Sulfonic Acid Derivatized Tryptic Peptides. Rapid Commun Mass Spectrom. 2001;15(23):2227-39. PubMed PMID: 11746890.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Atmospheric pressure matrix-assisted laser desorption/ionization ion trap mass spectrometry of sulfonic acid derivatized tryptic peptides. AU - Keough,T, AU - Lacey,M P, AU - Strife,R J, PY - 2001/12/18/pubmed PY - 2002/1/26/medline PY - 2001/12/18/entrez SP - 2227 EP - 39 JF - Rapid communications in mass spectrometry : RCM JO - Rapid Commun Mass Spectrom VL - 15 IS - 23 N2 - Atmospheric pressure matrix-assisted laser desorption/ionization (AP-MALDI) and ion trap mass spectrometry have been used to study the fragmentation behavior of native peptides and peptide derivatives prepared for de novo sequencing applications. Sulfonic acid derivatized peptides were observed to fragment more extensively and up to 28 times more efficiently than the corresponding native peptides. Tandem mass spectra of native peptides containing aspartic or glutamic acids are dominated by cleavage on the C-terminal side of the acidic residues. This significantly limits the amount of sequence information that can be derived from those compounds. The MS/MS spectra of native tryptic peptides containing oxidized Met residues show extensive loss of CH(3)SOH and little sequence-specific fragmentation. On the other hand, the tandem mass spectra of derivatized peptides containing Asp, Glu and oxidized Met show much more uniform fragmentation along the peptide backbone. The AP-MALDI tandem mass spectra of some derivatized peptides were shown to be qualitatively very similar to the corresponding vacuum MALDI postsource decay mass spectra, which were obtained on a reflector time-of-flight instrument. However, the ion trap mass spectrometer offers several advantages for peptide sequencing relative to current reflector time-of-flight instruments including improved product ion mass measurement accuracy, improved precursor ion selection and MS(n). These latter capabilities were demonstrated with solution digests of model proteins and with in-gel digests of 2D-gel separated proteins. SN - 0951-4198 UR - https://www.unboundmedicine.com/medline/citation/11746890/Atmospheric_pressure_matrix_assisted_laser_desorption/ionization_ion_trap_mass_spectrometry_of_sulfonic_acid_derivatized_tryptic_peptides_ L2 - https://doi.org/10.1002/rcm.499 DB - PRIME DP - Unbound Medicine ER -