The effect of histidine oxidation on the dissociation patterns of peptide ions

Bridgewater, Juma D.; Rapole, Srikanth; J, Lim; Vachet, Richard W.

doi:10.1016/j.jasms.2006.11.001

Cited by 28 publications

(34 citation statements)

References 50 publications

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“…Despite an incomplete understanding of the chemistry behind this labile modification, we have confidence in the site identification based upon the MS/MS data. Even though histidine modifications are unusual and none exist that are readily explained by a 15-Da increase, oxidation of histidines has been previously observed [28,29]. Fig.…”

Section: Characterization Of Photodegraded Mab-1mentioning

confidence: 82%

Investigation of degradation processes in IgG1 monoclonal antibodies by limited proteolysis coupled with weak cation-exchange HPLC

Lau

Pace

Yan

et al. 2010

Journal of Chromatography B

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Section: Characterization Of Photodegraded Mab-1mentioning

confidence: 82%

Investigation of degradation processes in IgG1 monoclonal antibodies by limited proteolysis coupled with weak cation-exchange HPLC

Lau

Pace

Yan

et al. 2010

Journal of Chromatography B

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“…Initial uses of HRPF were limited in spatial resolution to the size of a proteolytic peptide, as the amount of oxidation of any individual amino acid within the peptide could not be accurately quantified by CID [8-10]. As sub-microsecond HRPF technologies such as Fast Photochemical Oxidation of Proteins (FPOP) [3] and pulsed electron beam radiolysis [11] began to allow for heavier oxidation of proteins, the need to quantitate isomeric peptide oxidation products became even more pronounced.…”

Section: Introductionmentioning

confidence: 99%

Supercharging by m-NBA Improves ETD-Based Quantification of Hydroxyl Radical Protein Footprinting

Xie

et al. 2015

J. Am. Soc. Mass Spectrom.

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Hydroxyl radical protein footprinting (HRPF) is an MS-based technique for analyzing protein structure based on measuring the oxidation of amino acid side chains by hydroxyl radicals diffusing in solution. Spatial resolution of HRPF is limited by the smallest portion of the protein for which oxidation amounts can be accurately quantitated. Previous work has shown electron transfer dissociation (ETD) to be the most reliable method for quantifying the amount of oxidation of each amino acid side chain in a mixture of peptide oxidation isomers, but efficient ETD requires high peptide charge states which limits its applicability for HRPF. Supercharging reagents have been used to enhance peptide charge state for ETD analysis, but previous work have shown supercharging reagents to enhance charge state differently for different peptides sequences; it is currently unknown if different oxidation isomers will experience different charge enhancement effects. Here, we report the effect of m-nitrobenzyl alcohol (m-NBA) on the ETD-based quantification of peptide oxidation. The addition of m-NBA to both a defined mixture of synthetic isomeric oxidized peptides and Robo1 protein subjected to HRPF increased the abundance of higher charge state ions, improving our ability to perform efficient ETD of the mixture. No differences in the reported quantitation by ETD were noted in the presence or absence of m-NBA, indicating that all oxidation isomers were charge-enhanced to a similar extent. These results indicate the utility of m-NBA for residue-level quantification of peptide oxidation in HRPF and other applications.

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“…Also, methionine oxidation to methionine sulfoxide can cause peptide CID spectra to be dominated by a neutral loss of methane sulfenic acid (CH 3 SOH), which can limit sequence information [24 -28]. Very recently, histidine oxidation was also found to notably affect the dissociation pattern of peptides ions [29], complicating attempts to correctly sequence these peptides.To overcome the limited sequence information that is often found in the CID spectra of modified peptides, Address reprint requests to Dr. …”

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confidence: 99%

Improved sequencing of oxidized cysteine and methionine containing peptides using electron transfer dissociation

Rapole

Wilson

Bridgewater

et al. 2007

J. Am. Soc. Mass Spectrom.

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Oxidative modifications to the side chains of sulfur-containing amino acids often limit the number of product ions formed during collision-induced dissociation (CID) and thus make it difficult to obtain sequence information for oxidized peptides. In this work, we demonstrate that electron-transfer dissociation (ETD) can be used to improve the sequence information obtained from peptides with oxidized cysteine and methionine residues. In contrast to CID, ETD is found to be much less sensitive to the side-chain chemistry, enabling extensive sequence information to be obtained in cases where CID fails to provide this information. These results indicate that ETD is a valuable technique for studying oxidatively modified peptides and proteins. In addition, we report a unique and very abundant product ion that is formed in the CID spectra of peptides having N-terminal cysteine sulfinic acid residues. The mechanism for this unique dissociation pathway involves a six-membered cyclic intermediate and leads to the facile loss of NH 3 and SO 2 , which corresponds to a mass loss of 81 Da. While the facile nature of this dissociation pathway limits the sequence information present in CID spectra of peptides with N-terminal cysteine sulfinic acid residues, extensive sequence information for these peptides can be obtained with ETD. M ass spectrometry (MS) is widely used for sequencing and identifying amino acid modifications in peptides and proteins. Identifying modifications to proteins is important for a variety of reasons. Post-translational modifications (PTMs) of proteins are necessary for a wide range of cellular functions such as protein trafficking, protein-protein interactions, and transcription. Identifying and pinpointing these modification sites are important for more deeply understanding protein function, both normal and abnormal. In this context, PTMs such as phosphorylation, acetylation, glycosylation, sulfonation, and methylation are important to characterize. Oxidation is another important protein modification that is typically associated with oxidative stress [1-4], but recent work has also shown that protein oxidation can play a regulatory role as well [5]. Furthermore, an increasing number of techniques make use of oxidative labeling to study protein structure. These methods use radicals (e.g., · OH) to modify solvent-exposed [6 -9] or metal-bound amino acids [10 -17], and MS n to identify oxidatively modified residues, typically in conjunction with proteolytic digestion.Very often side-chain modifications to peptides can make sequencing by collision-induced dissociation (CID) difficult. Perhaps the most well known example is the effect of phosphorylation on peptide ion dissociation. The CID spectra of phosphorylated peptides are commonly dominated by a neutral loss of H 3 PO 4 , often with little other sequence information present. Similarly, side-chain oxidation can dramatically affect peptide dissociation patterns and limit sequence information that is available by CID. For example, oxidation of cysteine ...

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The effect of histidine oxidation on the dissociation patterns of peptide ions

Cited by 28 publications

References 50 publications

Investigation of degradation processes in IgG1 monoclonal antibodies by limited proteolysis coupled with weak cation-exchange HPLC

Investigation of degradation processes in IgG1 monoclonal antibodies by limited proteolysis coupled with weak cation-exchange HPLC

Supercharging by m-NBA Improves ETD-Based Quantification of Hydroxyl Radical Protein Footprinting

Improved sequencing of oxidized cysteine and methionine containing peptides using electron transfer dissociation

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