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Flame Atmospheric Pressure Chemical Ionization Coupled with Negative Electrospray Ionization Mass Spectrometry for Ion Molecule Reactions.

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Title: Flame Atmospheric Pressure Chemical Ionization Coupled with Negative Electrospray Ionization Mass Spectrometry for Ion Molecule Reactions.
Authors: Cheng, Sy-Chyi1, Bhat, Suhail1, Shiea, Jentaie jetea@mail.nsysu.edu.tw
Source: Journal of the American Society for Mass Spectrometry. Jul2017, Vol. 28 Issue 7, p1473-1481. 9p.
Subjects: Chemical ionization mass spectrometry, Ion-molecule collisions, Atmospheric pressure, Nitrates, Amino acids
Abstract: Flame atmospheric pressure chemical ionization (FAPCI) combined with negative electrospray ionization (ESI) mass spectrometry was developed to detect the ion/molecule reactions (IMRs) products between nitric acid (HNO) and negatively charged amino acid, angiotensin I (AI) and angiotensin II (AII), and insulin ions. Nitrate and HNO-nitrate ions were detected in the oxyacetylene flame, suggesting that a large quantity of nitric acid (HNO) was produced in the flame. The HNO and negatively charged analyte ions produced by a negative ESI source were delivered into each arm of a Y-shaped stainless steel tube where they merged and reacted. The products were subsequently characterized with an ion trap mass analyzer attached to the exit of the Y-tube. HNO showed the strongest affinity to histidine and formed (M-H+HNO) complex ions, whereas some amino acids did not react with HNO at all. Reactions between HNO and histidine residues in AI and AII resulted in the formation of dominant [M-H+(HNO)] and [M-H+(HNO)] ions. Results from analyses of AAs and insulin indicated that HNO could not only react with basic amino acid residues, but also with disulfide bonds to form [M-3H+(HNO)] complex ions. This approach is useful for obtaining information about the number of basic amino acid residues and disulfide bonds in peptides and proteins. [ABSTRACT FROM AUTHOR]
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Database: Engineering Source
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Abstract:Flame atmospheric pressure chemical ionization (FAPCI) combined with negative electrospray ionization (ESI) mass spectrometry was developed to detect the ion/molecule reactions (IMRs) products between nitric acid (HNO) and negatively charged amino acid, angiotensin I (AI) and angiotensin II (AII), and insulin ions. Nitrate and HNO-nitrate ions were detected in the oxyacetylene flame, suggesting that a large quantity of nitric acid (HNO) was produced in the flame. The HNO and negatively charged analyte ions produced by a negative ESI source were delivered into each arm of a Y-shaped stainless steel tube where they merged and reacted. The products were subsequently characterized with an ion trap mass analyzer attached to the exit of the Y-tube. HNO showed the strongest affinity to histidine and formed (M-H+HNO) complex ions, whereas some amino acids did not react with HNO at all. Reactions between HNO and histidine residues in AI and AII resulted in the formation of dominant [M-H+(HNO)] and [M-H+(HNO)] ions. Results from analyses of AAs and insulin indicated that HNO could not only react with basic amino acid residues, but also with disulfide bonds to form [M-3H+(HNO)] complex ions. This approach is useful for obtaining information about the number of basic amino acid residues and disulfide bonds in peptides and proteins. [ABSTRACT FROM AUTHOR]
ISSN:10440305
DOI:10.1007/s13361-017-1688-x