Detection, Number, and Sequence Location of Sulfur-Containing Amino Acids and Disulfide Bridges in Peptides by Ultrahigh-Resolution MALDI FTICR Mass Spectrometry

Touradj Solouki, Mark Emmett, Shengheng Guan, Alan G. Marshall

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Here, we present several strategies for determining the number of sulfur atoms and disulfide bridges in selected biologically active peptides, based on MALDIFTICR mass spectrometry at femtomole sample consumption level, first, based on the 2-Da mass increase per disulfide bridge reduction, we show that repeated laser shots on the same sample spot can reduce (and therefore reveal the presence of) the disulfide bridge in oxytocin. Second, we show that the primary sequence positions of the disulfide-bridged cystines can be inferred from the presence/absence of MALDI-induced reduction in cystine- containing fragment ions. Third, we show that the presence and number of sulfur atoms as well as the degree of reduction in a peptide can all be determined directly from isotopic relative abundances of mass-resolved 34S, 13C2, and reduced all-12C species in a single ultrahigh-resolution MALDI FTICR mass spectrum. Methods for achieving such ultrahigh mass resolution of peptide ions of closely spaced m/z (m/Δm50% ≈ 950 000 at m/z ≈ 650) at modest magnetic field (3 T) are discussed.

Original languageEnglish (US)
Pages (from-to)1163-1168
Number of pages6
JournalAnalytical Chemistry
Volume69
Issue number6
StatePublished - 1997
Externally publishedYes

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Sulfur
Disulfides
Mass spectrometry
Amino Acids
Peptides
Cystine
Ions
Atoms
Oxytocin
Magnetic fields
Lasers

ASJC Scopus subject areas

  • Analytical Chemistry

Cite this

Detection, Number, and Sequence Location of Sulfur-Containing Amino Acids and Disulfide Bridges in Peptides by Ultrahigh-Resolution MALDI FTICR Mass Spectrometry. / Solouki, Touradj; Emmett, Mark; Guan, Shengheng; Marshall, Alan G.

In: Analytical Chemistry, Vol. 69, No. 6, 1997, p. 1163-1168.

Research output: Contribution to journalArticle

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abstract = "Here, we present several strategies for determining the number of sulfur atoms and disulfide bridges in selected biologically active peptides, based on MALDIFTICR mass spectrometry at femtomole sample consumption level, first, based on the 2-Da mass increase per disulfide bridge reduction, we show that repeated laser shots on the same sample spot can reduce (and therefore reveal the presence of) the disulfide bridge in oxytocin. Second, we show that the primary sequence positions of the disulfide-bridged cystines can be inferred from the presence/absence of MALDI-induced reduction in cystine- containing fragment ions. Third, we show that the presence and number of sulfur atoms as well as the degree of reduction in a peptide can all be determined directly from isotopic relative abundances of mass-resolved 34S, 13C2, and reduced all-12C species in a single ultrahigh-resolution MALDI FTICR mass spectrum. Methods for achieving such ultrahigh mass resolution of peptide ions of closely spaced m/z (m/Δm50{\%} ≈ 950 000 at m/z ≈ 650) at modest magnetic field (3 T) are discussed.",
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AU - Guan, Shengheng

AU - Marshall, Alan G.

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AB - Here, we present several strategies for determining the number of sulfur atoms and disulfide bridges in selected biologically active peptides, based on MALDIFTICR mass spectrometry at femtomole sample consumption level, first, based on the 2-Da mass increase per disulfide bridge reduction, we show that repeated laser shots on the same sample spot can reduce (and therefore reveal the presence of) the disulfide bridge in oxytocin. Second, we show that the primary sequence positions of the disulfide-bridged cystines can be inferred from the presence/absence of MALDI-induced reduction in cystine- containing fragment ions. Third, we show that the presence and number of sulfur atoms as well as the degree of reduction in a peptide can all be determined directly from isotopic relative abundances of mass-resolved 34S, 13C2, and reduced all-12C species in a single ultrahigh-resolution MALDI FTICR mass spectrum. Methods for achieving such ultrahigh mass resolution of peptide ions of closely spaced m/z (m/Δm50% ≈ 950 000 at m/z ≈ 650) at modest magnetic field (3 T) are discussed.

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