Fragmentation of protonated ions of peptides containing cysteine, cysteine sulfinic acid, and cysteine sulfonic acid

Wang, Yinsheng; Shetty, Vivekananda; Men, Lijie; Zhang, Qibin

doi:10.1016/j.jasms.2004.01.005

Cited by 48 publications

(43 citation statements)

References 25 publications

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“…34,–38 Our findings are also consistent with previous CID work demonstrating that, under mobile-proton conditions, S -sulfonylation has little influence on critical energies. 48 By contrast, it has been reported that this modification can enhance fragmentation under charge-remote conditions for both ESI and fast atom bombardment-generated peptide ions. 48,49 However, we focus on multiply charged standard peptides with one or less arginines, and on tryptic peptide ions.…”

Section: Resultsmentioning

confidence: 95%

See 1 more Smart Citation

Targeted Annotation of S-Sulfonylated Peptides by Selective Infrared Multiphoton Dissociation Mass Spectrometry

et al. 2017

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Protein S-sulfinylation (R-SO2−) and S-sulfonylation (R-SO3−) are irreversible oxidative post-translational modifications of cysteine residues. Greater than 5% of cysteines are reported to occupy these higher oxidation states, which effectively inactivate the corresponding thiols and alter the electronic and physical properties of modified proteins. Such higher oxidation states are reached after excessive exposure to cellular oxidants, and accumulate across different disease states. Despite widespread and functionally relevant cysteine oxidation across the proteome, there are currently no robust methods to profile higher order cysteine oxidation. Traditional data-dependent liquid chromatography/tandem mass spectrometry (LC/MS/MS) methods generally miss low occupancy modifications in complex analyses. Here, we present a data-independent acquisition (DIA) LC/MS-based approach, leveraging the high IR absorbance of sulfoxides at 10.6 μm, for selective dissociation and discovery of S-sulfonated peptides. Across peptide standards and protein digests, we demonstrate selective infrared multiphoton dissociation (IRMPD) of S-sulfonated peptides in the background of unmodified peptides. This selective DIA IRMPD LC/MS-based approach allows identification and annotation of S-sulfonated peptides across complex mixtures while providing sufficient sequence information to localize the modification site.

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Section: Resultsmentioning

confidence: 95%

“…48 By contrast, it has been reported that this modification can enhance fragmentation under charge-remote conditions for both ESI and fast atom bombardment-generated peptide ions. 48,49 However, we focus on multiply charged standard peptides with one or less arginines, and on tryptic peptide ions.…”

Section: Resultsmentioning

confidence: 95%

Targeted Annotation of S-Sulfonylated Peptides by Selective Infrared Multiphoton Dissociation Mass Spectrometry

et al. 2017

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“…In each case, the active-site thiol was the most susceptible to HOSCN-induced sulfenic acid formation, with oxidation of other thiol residues on CK and GAPDH observed at higher oxidant concentrations. The MS/MS fragmentation patterns of Cys–SO 2 H-containing peptides are characteristically dominated by fragments corresponding to cleavage of the peptide C-terminal to the Cys–SO 2 H, in addition to an increased abundance of fragment ions originating from neutral losses of H 2 O and H 2 SO 2 , from the precursor and b n fragment ions [54,55]. For CK, the fragmentation spectra of the Cys-282 + 32 peptide is dominated by fragments corresponding to C-terminal Cys–SO 2 H cleavage ( b 17 ) and neutral losses (H 2 O, H 2 SO 2 ) from the [M + 2H] 2+ species.…”

Section: Discussionmentioning

confidence: 99%

Inactivation of thiol-dependent enzymes by hypothiocyanous acid: role of sulfenyl thiocyanate and sulfenic acid intermediates

Barrett

Pattison

Leonard

et al. 2012

Free Radical Biology and Medicine

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Myeloperoxidase (MPO) forms reactive oxidants including hypochlorous and hypothiocyanous acids (HOCl and HOSCN) under inflammatory conditions. HOCl causes extensive tissue damage and plays a role in the progression of many inflammatory-based diseases. Although HOSCN is a major MPO oxidant, particularly in smokers, who have elevated plasma thiocyanate, the role of this oxidant in disease is poorly characterized. HOSCN induces cellular damage by targeting thiols. However, the specific targets and mechanisms involved in this process are not well defined. We show that exposure of macrophages to HOSCN results in the inactivation of intracellular enzymes, including creatine kinase (CK) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). In each case, the active-site thiol residue is particularly sensitive to oxidation, with evidence for reversible inactivation and the formation of sulfenyl thiocyanate and sulfenic acid intermediates, on treatment with HOSCN (less than fivefold molar excess). Experiments with DAz-2, a cell-permeable chemical trap for sulfenic acids, demonstrate that these intermediates are formed on many cellular proteins, including GAPDH and CK, in macrophages exposed to HOSCN. This is the first direct evidence for the formation of protein sulfenic acids in HOSCN-treated cells and highlights the potential of this oxidant to perturb redox signaling processes.

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“…This peptide was oxidized using Fenton reagents (Fe +2 /H 2 O 2 ) as reported previously [36]. Briefly, 1 mM peptide solution was incubated at room temperature in the presence of 0.5 mM FeSO 4 and 0.2 mM H 2 O 2 for approximately 30 min.…”

Section: Methodsmentioning

confidence: 99%

Characterization of novel oxidation products of cysteine in an active site motif peptide of PTP1B

Shetty

Neubert

2009

J. Am. Soc. Mass Spectrom.

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We investigated the formation of hydroxyl radical (OH · ) and H 2 O 2 mediated oxidation products of a synthetic peptide, HCSAGIGRS, which is an active site sequence motif of protein tyrosine phosphatase 1B (PTP1B). We determined that a novel cysteine sulfinamide HC[S(O)N]SAGIGRS is produced in the oxidation reaction by Fenton reagents (Fe ϩ2 /H 2 O 2 ) as well as by H 2 O 2. These products were characterized by tandem mass spectrometry experiments on both singly and doubly charged precursor ions. MS 3 experiments using an ion trap instrument as well as LC-MS/MS experiments using a quadrupole time-of-flight (Q-TOF) instrument demonstrated that HC[S(O)N]SAGIGRS is not a water loss product of cysteine sulfinic acid [HC(SO 2 H)SAGIGRS]. We also obtained data from tandem mass spectrometry experiments that provided evidence for the existence of stable cysteine sulfenic acid [HC(SOH)SAGIGRS] in solution. A mechanism for the formation of the cysteine sulfinamide product is proposed based on the above experimental results. The preparation and identification of cysteine sulfinamide in this study may provide insight into the mechanism of both OH · and H 2 O 2 induced oxidation reactions of protein tyrosine phosphatases. (J Am Soc Mass Spectrom 2009, 20, 1540 -1548

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Fragmentation of protonated ions of peptides containing cysteine, cysteine sulfinic acid, and cysteine sulfonic acid

Cited by 48 publications

References 25 publications

Targeted Annotation of S-Sulfonylated Peptides by Selective Infrared Multiphoton Dissociation Mass Spectrometry

Targeted Annotation of S-Sulfonylated Peptides by Selective Infrared Multiphoton Dissociation Mass Spectrometry

Inactivation of thiol-dependent enzymes by hypothiocyanous acid: role of sulfenyl thiocyanate and sulfenic acid intermediates

Characterization of novel oxidation products of cysteine in an active site motif peptide of PTP1B

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