Identification of Oxidized Methionine in Peptides

Lagerwerf, Fija M.; Weert, Marco van de; Heerma, W.; Haverkamp, Johan

doi:10.1002/(sici)1097-0231(199612)10:15<1905::aid-rcm755>3.0.co;2-9

Cited by 113 publications

(87 citation statements)

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“…Oxidation of cysteine to cysteine sulfinic acid also leads to selective dissociation on the C-terminal side of this residue when the peptide charge state does not exceed the number of arginine residues in the peptide [23,24]. Methionine oxidation to methionine sulfoxide can have a dramatic effect on peptide ion dissociation patterns too [25][26][27][28][29]. When the number of protons on the peptide does not exceed the number of basic residues, product ion spectra of peptides containing methionine sulfoxide are dominated by a neutral loss of methane sulfenic acid (CH 3 SOH) [29].…”

Section: Introductionmentioning

confidence: 99%

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

Bridgewater

Rapole

et al. 2007

J. Am. Soc. Mass Spectrom.

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Oxidative modifications to amino acid side chains can change the dissociation pathways of peptide ions, but these variations are most commonly observed when cysteine and methionine residues are oxidized. In this work we describe the very noticeable effect that oxidation of histidine residues can have on the dissociation patterns of peptide ions containing this residue. A common product ion spectral feature of doubly-charged tryptic peptides is enhanced cleavage at the C-terminal side of histidine residues. This preferential cleavage arises due to the unique acid/base character of the imidazole side chain that initiates cleavage of a proximal peptide bond for ions in which the number of protons does not exceed the number of basic residues. We demonstrate here that this enhanced cleavage is eliminated when histidine is oxidized to 2-oxo-histidine because the proton affinity and nucleophilicity of the imidazole side chain are lowered. Furthermore, we find that oxidation of histidine to 2-oxo-histidine can cause the mis-assignment of oxidized residues when more than one oxidized isomer is simultaneously subjected to tandem mass spectrometry (MS/MS). These spectral misinterpretations can be avoided usually by using multiple stages of MS/MS (MS n ) or via speciallyoptimized liquid chromatographic separation conditions. When these approaches are not accessible or do not work, N-terminal derivatization with sulfobenzoic acid avoids the problem of mistakenly assigning oxidized residues.

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Section: Introductionmentioning

confidence: 99%

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

Bridgewater

Rapole

et al. 2007

J. Am. Soc. Mass Spectrom.

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“…Moreover a neutral loss of 64 amu from the parent ion at m/z 1814.9 1ϩ observed in the MS/MS spectrum of the modified peptide (Fig. 1C) was indicative of neutral loss of methanesulfenic acid from methionine sulfoxide (50).…”

Section: Characterization Of Modifications Detected On the Peptide Spmentioning

confidence: 71%

“…1C and 3C), indicated conversion of methionine to methionine sulfoxide, which is a commonly observed phenomenon during storage and sample handling (50). A characteristic neutral loss of 64 amu was observed from both of these peptides due to the elimination of methanesulfenic acid (CH 3 SOH, Ϫ64 amu) as an indicator for the presence of oxidized methionine (50).…”

Section: Discussionmentioning

confidence: 99%

Sulfonation and Phosphorylation of Regions of the Dioxin Receptor Susceptible to Methionine Modifications

Dave

Whelan

Bindloss

et al. 2009

Molecular & Cellular Proteomics

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“…The integral intensity of y-series is significantly higher than that of b-series due to the presence of two basic arginines at the C-terminus of brevinin-1Ra. The characteristic neutral loss of 80 Da (MeSO 2 H) is also observed [29]. This loss indicates the presence of oxidized methionine in the peptide sequence.…”

Section: Brevinin-1ava and Brevinin-1ramentioning

confidence: 85%

Oxidation versus carboxamidomethylation of s-s bond in ranid frog peptides: Pro and contra for de novo MALDI-MS sequencing

Samgina

Artemenko

Gorshkov

et al. 2008

J. Am. Soc. Mass Spectrom.

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Five natural peptides isolated from ranid skin secretions of European frog species of Rana ridibunda and Rana arvalis (molecular masses 3516, 26743516, , 26363516, , 18743516, , and 1810 were studied by MALDI-TOF/TOF to compare two procedures of disulfide bond cleavage: (1) performic oxidation and (2) reduction/carboxamidomethylation. The processes are relevant for the elucidation of the amino acid sequence inside the seven-member cystine ring at the C-terminus. The results clearly demonstrated that oxidation of the disulfide bond led to notably higher abundances of b-and y-ions, corresponding to the C-terminal peptide bonds, than reduction/carboxamidomethylation. This conclusion is true for all five peptides studied. Besides that, the oxidation procedure is simpler than carboxamidomethylation, as it is a one-step process with no purification required. The oxidation is more reproducible. The results were similar each time the peptide was subjected to the process. It was successfully applied to all five peptides while reduction/carboxamidomethylation failed in the case of brevinin-1Ra, despite all variations of reaction conditions. (J Am Soc Mass Spectrom 2008, 19, 479 -487) © 2008 American Society for Mass Spectrometry A skin secretion produced by granular skin glands of anurans in response to a variety of stimuli contains biologically active peptides [1][2][3][4]. Our interest was focused on the Rana genus containing a notable array of common frogs spread around the territory of Eurasia and America. A major part of ranid peptides has a disulfide cycle at the C-terminus [1,5]. This peculiarity, called "Rana box" [6], complicates sequencing of these peptides. The amino acid sequence inside the cycle is practically unattainable by means of mass spectrometry without preliminary chemical derivatization. There is only one communication on direct sequence identification inside the C-terminus disulfide cycle using ESI MS/MS in the negative ion mode. It deals with some bioactive peptides isolated from genus Crinia (Australia) and with brevinin-1E R. ridibunda, (Russia) [7]. In this case, a combination of the positive and negative mass spectra has produced complete sequences for all the investigated peptides. Unfortunately not all peptides give reasonable negative ion spectra.Mass spectrometric sequencing of disulfide containing peptides requires preliminary modification of the S-S bond. There are two general methods to cleave this bond: (1) reduction followed by the alkylation of cysteines [8 -10]; (2) oxidation with performic acid [11]. The first procedure is traditionally used to break S-S bonds in proteins with associated polypeptide chains before their enzymatic digestion. We applied it for the skin peptides of the Rana genus with an internal disulfide cycle [12,13]. Reduction of the S-S bond followed by carboxamidomethylation allows reliable sequencing at the C-terminus. LTQ FTICR mass spectrometric results completely match those obtained by Edman degradation.Performic oxidation is a well-known method for the cl...

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Identification of Oxidized Methionine in Peptides

Cited by 113 publications

References 0 publications

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

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

Sulfonation and Phosphorylation of Regions of the Dioxin Receptor Susceptible to Methionine Modifications

Oxidation versus carboxamidomethylation of s-s bond in ranid frog peptides: Pro and contra for de novo MALDI-MS sequencing

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