Disulfide bond cleavage in TEMPO-free radical initiated peptide sequencing mass spectrometry

The gas‐phase free radical initiated peptide sequencing (FRIPS) fragmentation behavior of o‐TEMPO‐Bz‐conjugated peptides with an intra‐ and intermolecular disulfide bond was investigated using MSn tandem mass spectrometry experiments. Investigated peptides included four peptides with an intramolecul...

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Published in	Journal of mass spectrometry. Vol. 46; no. 8; pp. 830 - 839
Main Authors	Lee, Minhee, Lee, Younjin, Kang, Minhyuk, Park, Hyeyeon, Seong, Yeonmi, June Sung, Bong, Moon, Bongjin, Bin Oh, Han
Format	Journal Article
Language	English
Published	Chichester, UK John Wiley & Sons, Ltd 01.08.2011 Wiley
Subjects	Adrenomedullin - chemistry Amino Acid Sequence Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Biological and medical sciences Bonding Cleavage disulfide bond cleavage Disulfides Disulfides - analysis Disulfides - chemistry Disulfides - metabolism Fragmentation Fragments free radical initiated peptide sequencing Free Radicals - chemistry Fundamental and applied biological sciences. Psychology Humans Hypothalamic Hormones - chemistry Mass spectrometry Melanins - chemistry Molecular Sequence Data odd-electron tandem mass spectrometry peptide sequencing Peptides Peptides, Cyclic - chemistry Pituitary Hormones - chemistry Proteins Radicals Sequence Analysis, Protein - methods Tandem Mass Spectrometry - methods TEMPO Transforming Growth Factor alpha - chemistry Tandem mass spectrometry Nitroxyl Reaction path Fragmentation pattern Primary structure free radical initiated peptide sequencing Peptide map disulfide bond cleavage peptide sequencing Disulfide bond Organic free radical Cleavage odd-electron tandem mass spectrometry Gas phase TEMPO Mass spectrometry Aminoacid sequence Structural analysis
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Abstract	The gas‐phase free radical initiated peptide sequencing (FRIPS) fragmentation behavior of o‐TEMPO‐Bz‐conjugated peptides with an intra‐ and intermolecular disulfide bond was investigated using MSn tandem mass spectrometry experiments. Investigated peptides included four peptides with an intramolecular cyclic disulfide bond, Bactenecin (RLCRIVVIRVCR), TGF‐α (CHSGYVGVRC), MCH (DFDMLRCMLGRVFRPCWQY) and Adrenomedullin (16–31) (CRFGTCTVQKLAHQIY), and two peptides with an intermolecular disulfide bond. Collisional activation of the benzyl radical conjugated peptide cation, which was generated through the release of a TEMPO radical from o‐TEMPO‐Bz‐conjugated peptides upon initial collisional activation, produced a large number of peptide backbone fragments in which the SS or CS bond was readily cleaved. The observed peptide backbone fragments included a‐, c‐, x‐ or z‐types, which indicates that the radical‐driven peptide fragmentation mechanism plays an important role in TEMPO‐FRIPS mass spectrometry. FRIPS application of the linearly linked disulfide peptides further showed that the SS or CS bond was selectively and preferentially cleaved, followed by peptide backbone dissociations. In the FRIPS mass spectra, the loss of •SH or •SSH was also abundantly found. On the basis of these findings, FRIPS fragmentation pathways for peptides with a disulfide bond are proposed. For the cleavage of the SS bond, the ion of a hydrogen atom at Cβ by the benzyl radical is proposed to be the initial radical ion/transfer reaction. On the other hand, H‐ion at Cα is suggested to lead to CS bond cleavage, which yields [ion ± S] fragments or the loss of •SH or •SSH. Copyright © 2011 John Wiley & Sons, Ltd.
AbstractList	The gas‐phase free radical initiated peptide sequencing (FRIPS) fragmentation behavior of o‐TEMPO‐Bz‐conjugated peptides with an intra‐ and intermolecular disulfide bond was investigated using MSn tandem mass spectrometry experiments. Investigated peptides included four peptides with an intramolecular cyclic disulfide bond, Bactenecin (RLCRIVVIRVCR), TGF‐α (CHSGYVGVRC), MCH (DFDMLRCMLGRVFRPCWQY) and Adrenomedullin (16–31) (CRFGTCTVQKLAHQIY), and two peptides with an intermolecular disulfide bond. Collisional activation of the benzyl radical conjugated peptide cation, which was generated through the release of a TEMPO radical from o‐TEMPO‐Bz‐conjugated peptides upon initial collisional activation, produced a large number of peptide backbone fragments in which the SS or CS bond was readily cleaved. The observed peptide backbone fragments included a‐, c‐, x‐ or z‐types, which indicates that the radical‐driven peptide fragmentation mechanism plays an important role in TEMPO‐FRIPS mass spectrometry. FRIPS application of the linearly linked disulfide peptides further showed that the SS or CS bond was selectively and preferentially cleaved, followed by peptide backbone dissociations. In the FRIPS mass spectra, the loss of •SH or •SSH was also abundantly found. On the basis of these findings, FRIPS fragmentation pathways for peptides with a disulfide bond are proposed. For the cleavage of the SS bond, the ion of a hydrogen atom at Cβ by the benzyl radical is proposed to be the initial radical ion/transfer reaction. On the other hand, H‐ion at Cα is suggested to lead to CS bond cleavage, which yields [ion ± S] fragments or the loss of •SH or •SSH. Copyright © 2011 John Wiley & Sons, Ltd. The gas-phase free radical initiated peptide sequencing (FRIPS) fragmentation behavior of o-TEMPO-Bz-conjugated peptides with an intra- and intermolecular disulfide bond was investigated using MSn tandem mass spectrometry experiments. Investigated peptides included four peptides with an intramolecular cyclic disulfide bond, Bactenecin (RLCRIVVIRVCR), TGF- (CHSGYVGVRC), MCH (DFDMLRCMLGRVFRPCWQY) and Adrenomedullin (16-31) (CRFGTCTVQKLAHQIY), and two peptides with an intermolecular disulfide bond. Collisional activation of the benzyl radical conjugated peptide cation, which was generated through the release of a TEMPO radical from o-TEMPO-Bz-conjugated peptides upon initial collisional activation, produced a large number of peptide backbone fragments in which the SS or CS bond was readily cleaved. The observed peptide backbone fragments included a-, c-, x- or z-types, which indicates that the radical-driven peptide fragmentation mechanism plays an important role in TEMPO-FRIPS mass spectrometry. FRIPS application of the linearly linked disulfide peptides further showed that the SS or CS bond was selectively and preferentially cleaved, followed by peptide backbone dissociations. In the FRIPS mass spectra, the loss of -SH or -SSH was also abundantly found. On the basis of these findings, FRIPS fragmentation pathways for peptides with a disulfide bond are proposed. For the cleavage of the SS bond, the abstraction of a hydrogen atom at C Delta *b by the benzyl radical is proposed to be the initial radical abstraction/transfer reaction. On the other hand, H-abstraction at C is suggested to lead to CS bond cleavage, which yields [ion ? S] fragments or the loss of -SH or -SSH. The gas-phase free radical initiated peptide sequencing (FRIPS) fragmentation behavior of o-TEMPO-Bz-conjugated peptides with an intra- and intermolecular disulfide bond was investigated using MS(n) tandem mass spectrometry experiments. Investigated peptides included four peptides with an intramolecular cyclic disulfide bond, Bactenecin (RLCRIVVIRVCR), TGF-α (CHSGYVGVRC), MCH (DFDMLRCMLGRVFRPCWQY) and Adrenomedullin (16-31) (CRFGTCTVQKLAHQIY), and two peptides with an intermolecular disulfide bond. Collisional activation of the benzyl radical conjugated peptide cation, which was generated through the release of a TEMPO radical from o-TEMPO-Bz-conjugated peptides upon initial collisional activation, produced a large number of peptide backbone fragments in which the S-S or C-S bond was readily cleaved. The observed peptide backbone fragments included a-, c-, x- or z-types, which indicates that the radical-driven peptide fragmentation mechanism plays an important role in TEMPO-FRIPS mass spectrometry. FRIPS application of the linearly linked disulfide peptides further showed that the S-S or C-S bond was selectively and preferentially cleaved, followed by peptide backbone dissociations. In the FRIPS mass spectra, the loss of •SH or •SSH was also abundantly found. On the basis of these findings, FRIPS fragmentation pathways for peptides with a disulfide bond are proposed. For the cleavage of the S-S bond, the abstraction of a hydrogen atom at C(β) by the benzyl radical is proposed to be the initial radical abstraction/transfer reaction. On the other hand, H-abstraction at C(α) is suggested to lead to C-S bond cleavage, which yields [ion ± S] fragments or the loss of •SH or •SSH. Abstract The gas‐phase free radical initiated peptide sequencing (FRIPS) fragmentation behavior of o ‐TEMPO‐Bz‐conjugated peptides with an intra‐ and intermolecular disulfide bond was investigated using MS n tandem mass spectrometry experiments. Investigated peptides included four peptides with an intramolecular cyclic disulfide bond, Bactenecin (RL C RIVVIRV C R), TGF‐α ( C HSGYVGVR C ), MCH (DFDMLR C MLGRVFRP C WQY) and Adrenomedullin (16–31) ( C RFGT C TVQKLAHQIY), and two peptides with an intermolecular disulfide bond. Collisional activation of the benzyl radical conjugated peptide cation, which was generated through the release of a TEMPO radical from o ‐TEMPO‐Bz‐conjugated peptides upon initial collisional activation, produced a large number of peptide backbone fragments in which the SS or CS bond was readily cleaved. The observed peptide backbone fragments included a ‐, c ‐, x ‐ or z ‐types, which indicates that the radical‐driven peptide fragmentation mechanism plays an important role in TEMPO‐FRIPS mass spectrometry. FRIPS application of the linearly linked disulfide peptides further showed that the SS or CS bond was selectively and preferentially cleaved, followed by peptide backbone dissociations. In the FRIPS mass spectra, the loss of •SH or •SSH was also abundantly found. On the basis of these findings, FRIPS fragmentation pathways for peptides with a disulfide bond are proposed. For the cleavage of the SS bond, the abstraction of a hydrogen atom at C β by the benzyl radical is proposed to be the initial radical abstraction/transfer reaction. On the other hand, H‐abstraction at C α is suggested to lead to CS bond cleavage, which yields [ion ± S] fragments or the loss of •SH or •SSH. Copyright © 2011 John Wiley & Sons, Ltd.
Author	Moon, Bongjin Lee, Younjin Park, Hyeyeon June Sung, Bong Bin Oh, Han Kang, Minhyuk Seong, Yeonmi Lee, Minhee
Author_xml	– sequence: 1 givenname: Minhee surname: Lee fullname: Lee, Minhee organization: Department of Chemistry, Sogang University, Seoul 121-742, Korea – sequence: 2 givenname: Younjin surname: Lee fullname: Lee, Younjin organization: Department of Chemistry, Sogang University, Seoul 121-742, Korea – sequence: 3 givenname: Minhyuk surname: Kang fullname: Kang, Minhyuk organization: Department of Chemistry, Sogang University, Seoul 121-742, Korea – sequence: 4 givenname: Hyeyeon surname: Park fullname: Park, Hyeyeon organization: Department of Chemistry, Sogang University, Seoul 121-742, Korea – sequence: 5 givenname: Yeonmi surname: Seong fullname: Seong, Yeonmi organization: Department of Chemistry, Sogang University, Seoul 121-742, Korea – sequence: 6 givenname: Bong surname: June Sung fullname: June Sung, Bong organization: Department of Chemistry, Sogang University, Seoul 121-742, Korea – sequence: 7 givenname: Bongjin surname: Moon fullname: Moon, Bongjin organization: Department of Chemistry, Sogang University, Seoul 121-742, Korea – sequence: 8 givenname: Han surname: Bin Oh fullname: Bin Oh, Han email: hanbinoh@sogang.ac.kr organization: Department of Chemistry, Sogang University, Seoul 121-742, Korea
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Keywords	Tandem mass spectrometry Nitroxyl Reaction path Fragmentation pattern Primary structure free radical initiated peptide sequencing Peptide map disulfide bond cleavage peptide sequencing Disulfide bond Organic free radical Cleavage odd-electron tandem mass spectrometry Gas phase TEMPO Mass spectrometry Aminoacid sequence Structural analysis
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Snippet	The gas‐phase free radical initiated peptide sequencing (FRIPS) fragmentation behavior of o‐TEMPO‐Bz‐conjugated peptides with an intra‐ and intermolecular... The gas-phase free radical initiated peptide sequencing (FRIPS) fragmentation behavior of o-TEMPO-Bz-conjugated peptides with an intra- and intermolecular... Abstract The gas‐phase free radical initiated peptide sequencing (FRIPS) fragmentation behavior of o ‐TEMPO‐Bz‐conjugated peptides with an intra‐ and...
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SubjectTerms	Adrenomedullin - chemistry Amino Acid Sequence Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Biological and medical sciences Bonding Cleavage disulfide bond cleavage Disulfides Disulfides - analysis Disulfides - chemistry Disulfides - metabolism Fragmentation Fragments free radical initiated peptide sequencing Free Radicals - chemistry Fundamental and applied biological sciences. Psychology Humans Hypothalamic Hormones - chemistry Mass spectrometry Melanins - chemistry Molecular Sequence Data odd-electron tandem mass spectrometry peptide sequencing Peptides Peptides, Cyclic - chemistry Pituitary Hormones - chemistry Proteins Radicals Sequence Analysis, Protein - methods Tandem Mass Spectrometry - methods TEMPO Transforming Growth Factor alpha - chemistry
Title	Disulfide bond cleavage in TEMPO-free radical initiated peptide sequencing mass spectrometry
URI	https://api.istex.fr/ark:/67375/WNG-SW16567D-C/fulltext.pdf https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fjms.1955 https://www.ncbi.nlm.nih.gov/pubmed/21834022 https://search.proquest.com/docview/1022863990 https://search.proquest.com/docview/883308213
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