Negative ion fragmentations of disulfide‐containing cross‐linking reagents are competitive with aspartic acid side‐chain‐induced cleavages

Calabrese, Antonio N.; Wang, Tianfang; Bowie, John H.; Pukala, Tara L.

doi:10.1002/rcm.6445

Cited by 6 publications

(5 citation statements)

References 47 publications

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“…A recent report details a development in which CID is used in parallel with electron-capture dissociation (ECD): CID cleaves the linker at a predictable site to generate reporter ions, while ECD does not induce linker cleavage and instead provides peptide sequence information [131]. In addition, disulfide-targeted cross-linking reagents have been developed which cleave only in negative ion mode, allowing for complimentary analyses on a single sample [133]. …”

Section: Structural and Kinetic Investigations Of Thiol Proteins Bmentioning

confidence: 99%

Mass spectrometry in studies of protein thiol chemistry and signaling: Opportunities and caveats

Baez

Reisz

Furdui

2015

Free Radical Biology and Medicine

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Mass spectrometry (MS) has become a powerful and widely utilized tool in the investigation of protein thiol chemistry, biochemistry, and biology. Very early biochemical studies of metabolic enzymes have brought to light the broad spectrum of reactivity profiles that distinguish cysteine thiols with functions in catalysis and protein stability from other cysteine residues in proteins. The development of MS methods for the analysis of proteins using electrospray ionization (ESI) or matrix-assisted laser desorption/ionization (MALDI) coupled with the emergence of high-resolution mass analyzers have been instrumental in advancing studies of thiol modifications, both in single proteins and within the cellular context. This article reviews MS instrumentation and methods of analysis employed in investigations of thiols and their reactivity toward a range of small biomolecules. A selected number of studies are detailed to highlight the advantages brought about by the MS technologies along with the caveats associated with these analyses.

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Section: Structural and Kinetic Investigations Of Thiol Proteins Bmentioning

confidence: 99%

Mass spectrometry in studies of protein thiol chemistry and signaling: Opportunities and caveats

Baez

Reisz

Furdui

2015

Free Radical Biology and Medicine

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“…All the octapeptides used in this work are listed in Table 1. Oxidized disulfide-containing forms were obtained by oxidations of the dithiol peptides, [24][25][26][27][28] and were investigated accordingly. We herein report the results obtained.…”

Section: Introductionmentioning

confidence: 99%

Mass spectral and theoretical investigations of N–C^αbond cleavages in the disulfide‐containing peptide TTCPYCKK and its analogues

Wang

Tian

et al. 2022

Rapid Comm Mass Spectrometry

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Rationale For disulfide‐containing peptides, mass spectrometric analyses are rarely comparably studied between their dithiol and disulfide forms. Persulfide ions afforded from peptides with a disulfide ring are from either an unusual N–Cα bond cleavage or a canonical peptide bond cleavage; their isomeric structures are, however, not identified just from peaks of mass spectra. Methods Isomeric structures of [C3P4X5|C6M], [C3MAP4X5|C6MB] and [P4X5C6|C3M] were identified from a series of the X5 substituted dicysteine octapeptides using electrospray ionization tandem mass spectrometry for both their dithiol and disulfide forms. Formation mechanisms of different persulfide ions were investigated systematically by theoretical methods. Moreover, electrostatic potential‐mapped molecular van der Waals surfaces were used to determine the stabilities of the intermediates, which gave a further evaluation of favored bond cleavage. Results Mass spectral analyses indicated that the fragmented ions changed largely when an intramolecular disulfide bond was formed. New types of disulfide‐containing fragmented ions [C3P4X5|C6M] or [C3MAP4X5|C6MB] were thus proposed. Energy analysis showed that the N–Cα cleavage was not competitive energetically with that of the amide bond for Y5 and its phosphorylated analogue. However, the N–Cα cleavage products dominated for the S5‐ and T5‐containing peptides. Stabilities of the intermediates were found to be related with the electrostatic potential‐mapped molecular van der Waals surfaces. Conclusions Persulfide ions containing more residues than previously found were proposed not only from b7 ions but also from y6 ions. In addition, a new kind of phosphorylated analogue, [C3P4pY5|C6M], is reported in this work. Our study provides convincing results for separating isomeric structures in the cases of N–Cα cleavages, which greatly assists in the structural identification of disulfide‐containing peptides.

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“…The structures of the other intermolecular peptides shown in Scheme are determined in similar fashion. The facile negative‐ion cleavages of the intermolecular disulfide group have also been used to identify cross‐linked peptides and proteins (Calabrese et al, , ).…”

Section: Introductionmentioning

confidence: 99%

Negative ion cleavages of (M–H)⁻ anions of peptides. Part 3. Post‐translational modifications

Wang

Tran

Andreazza

et al. 2016

Mass Spectrometry Reviews

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It is now 25 years since we commenced the study of the negative-ion fragmentations of peptides and we have recently concluded this research with investigations of the negative-ion chemistry of most post-translational functional groups. Our first negative-ion peptide review (Bowie, Brinkworth, & Dua, 2002) dealt with the characteristic backbone fragmentations and side-chain cleavages from (M-H) ions of underivatized peptides, while the second (Bilusich & Bowie, 2009) included negative-ion backbone cleavages for Ser and Cys and some initial data on some post-translational groups including disulfides. This third and final review provides a brief summary of the major backbone and side chain cleavages outlined before (Bowie, Brinkworth, & Dua, 2002) and describes the quantum mechanical hydrogen tunneling associated with some proton transfers in enolate anion/enolate systems. The review then describes, in more depth, the negative-ion cleavages of the post-translational groups Kyn, isoAsp, pyroglu, disulfides, phosphates, and sulfates. Particular emphasis is devoted to disulfides (both intra- and intermolecular) and phosphates because of the extensive and spectacular anion chemistry shown by these groups. © 2016 Wiley Periodicals, Inc. Mass Spec Rev.

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Negative ion fragmentations of disulfide‐containing cross‐linking reagents are competitive with aspartic acid side‐chain‐induced cleavages

Cited by 6 publications

References 47 publications

Mass spectrometry in studies of protein thiol chemistry and signaling: Opportunities and caveats

Mass spectrometry in studies of protein thiol chemistry and signaling: Opportunities and caveats

Mass spectral and theoretical investigations of N–C^αbond cleavages in the disulfide‐containing peptide TTCPYCKK and its analogues

Negative ion cleavages of (M–H)⁻ anions of peptides. Part 3. Post‐translational modifications

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Negative ion fragmentations of disulfide‐containing cross‐linking reagents are competitive with aspartic acid side‐chain‐induced cleavages

Cited by 6 publications

References 47 publications

Mass spectrometry in studies of protein thiol chemistry and signaling: Opportunities and caveats

Mass spectrometry in studies of protein thiol chemistry and signaling: Opportunities and caveats

Mass spectral and theoretical investigations of N–Cαbond cleavages in the disulfide‐containing peptide TTCPYCKK and its analogues

Negative ion cleavages of (M–H)− anions of peptides. Part 3. Post‐translational modifications

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Mass spectral and theoretical investigations of N–C^αbond cleavages in the disulfide‐containing peptide TTCPYCKK and its analogues

Negative ion cleavages of (M–H)⁻ anions of peptides. Part 3. Post‐translational modifications