High‐throughput method for on‐target performic acid oxidation of MALDI‐deposited samples

Williams, Brad J.; Russell, William K.; Russell, David H.

doi:10.1002/jms.1699

Cited by 7 publications

(7 citation statements)

References 27 publications

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“…In addition, the detection of the various states of cysteine oxidation-i.e., disulfide bonds (-S-S-), sulfenic (-SOH), sulfinic (-SO 2 H) or sulfonic (-SO 3 H) acidsis becoming increasingly important in many biological processes, including oxidative stress [9][10][11][12]. Sulfonic acid is the final oxidation product of many such processes, and negative ion MS has proven effective for the detection of [M -H] − ions from cysteic-acid-containing peptides [13][14][15]. To date, a limited number of studies on negative ion fragmentation of cysteic-acid-containing peptides have been reported [14].…”

Section: ) From the Parent [M -H]mentioning

confidence: 99%

“…Dual protease digestion (trypsin followed by chymotrypsin) of RNase A was performed using previously described methods [15,21]. Briefly, RNase A was dissolved at 1 mg mL −1 in a 25 mM ammonium acetate buffer adjusted to pH 6.0 with 10 mM formic acid.…”

Section: Ribonuclease a Proteolytic Digestionmentioning

confidence: 99%

“…On-target performic acid oxidation was performed as described previously [15]. Briefly, 40 μL of a 1:1 mixture of acetone: performic acid was placed directly on the MALDI target in a region that does not contain sample.…”

Section: On-target Performic Acid Oxidationmentioning

confidence: 99%

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Effect of Cysteic Acid Position on the Negative Ion Fragmentation of Proteolytic Derived Peptides

Williams

Kmiec

Russell

et al. 2011

J. Am. Soc. Mass Spectrom.

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A study on the effect of cysteic acid position on the types of fragment ions formed by collisioninduced dissociation (CID) of [M -H] − ions is presented. Of particular note is the observation of d-type fragment ions for peptides that contain an N-terminal cysteic acid (fixed negative charge) and cleavable amino acid side chains possessing a β-γ carbon-carbon bond. For example, the CID mass spectrum of oxidized cys-kemptide (C ox LRRASLG) [M -H + O 3 ] − ions contains abundant series of d-type fragment ions, and similar results are observed for oxidized cysteinecontaining ribonuclease A proteolytic peptides. The d i fragment ions are assumed to arise by a charge-remote and/or charge-assisted fragmentation mechanism, which both occur at high collision energies and involve consecutive reactions (i.e., the formation of a i ions followed by the elimination of the side chain to form d i ions).

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Section: ) From the Parent [M -H]mentioning

confidence: 99%

Section: Ribonuclease a Proteolytic Digestionmentioning

confidence: 99%

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Effect of Cysteic Acid Position on the Negative Ion Fragmentation of Proteolytic Derived Peptides

Williams

Kmiec

Russell

et al. 2011

J. Am. Soc. Mass Spectrom.

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“…al . 39 only cysteine residues are affected by the treatment, and the on-target oxidation is not complicated by reactions with H, M, W or Y amino acid containing peptides.…”

Section: Resultsmentioning

confidence: 99%

Cycloquest: Identification of Cyclopeptides via Database Search of Their Mass Spectra against Genome Databases

Mohimani

Liu

Mylne³

et al. 2011

J. Proteome Res.

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Hundreds of ribosomally synthesized cyclopeptides have been isolated from all domains of life, the vast majority having been reported in the last 15 years. Studies of cyclic peptides have highlighted their exceptional potential both as stable drug scaffolds and as biomedicines in their own right. Despite this, computational techniques for cyclopeptide identification are still in their infancy, with many such peptides remaining uncharacterized. Tandem mass spectrometry has occupied a niche role in cyclopeptide identification, taking over from traditional techniques such as nuclear magnetic resonance spectroscopy (NMR). MS/MS studies require only picogram quantities of peptide (compared to milligrams for NMR studies) and are applicable to complex samples, abolishing the requirement for time-consuming chromatographic purification. While database search tools such as Sequest and Mascot have become standard tools for the MS/MS identification of linear peptides, they are not applicable to cyclopeptides, due to the parent mass shift resulting from cyclization, and different fragmentation pattern of cyclic peptides. In this paper, we describe the development of a novel database search methodology to aid in the identification of cyclopeptides by mass spectrometry, and evaluate its utility in identifying two peptide rings from Helianthus annuus, a bacterial cannibalism factor from Bacillus subtilis, and a θ-defensin from Rhesus macaque.

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“…The model peptides containing cysteine residues were oxidized using solution-phase performic acid oxidation as previously described [25,26]. Briefly, 50 μL of performic acid (1:19 hydrogen peroxide:formic acid) was used to resuspend ca.…”

Section: Solution-phase Performic Acid Oxidationmentioning

confidence: 99%

Negative Ion Fragmentation of Cysteic Acid Containing Peptides: Cysteic Acid as a Fixed Negative Charge

Williams

Barlow

Kmiec

et al. 2011

J. Am. Soc. Mass Spectrom.

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We present here a study of the collision induced dissociation (CID) of deprotonated cysteic acid containing peptides produced by MALDI. The effect of cysteic acid (C ox ) position is interrogated by considering the positional isomers, C ox LVINVLSQG, LVINVLSQGC ox , and LVINVC ox LSQG. Although considerable variation between the CID spectra is observed, the mechanistic picture that emerges involves charge retention at the deprotonated cysteic acid side chain. Fragmentation occurs in the proximity of the cysteic acid group by charge directed mechanisms as well as remote from this group to form ions, which may be rationalized by charge remote mechanisms. Additionally, the formation of the SO 3 -• ion is observed in all cases. Fragmentation of C ox LVINVLSQC ox provides both N-and C-terminal, y and b ions, respectively indicating that the negative charge may be retained at either of the cysteic acids; however, there is some evidence that charge retention at the C-terminal cysteic acid may be preferred. Fragmentation of tryptic type peptides containing a C-terminal arginine or lysine residue is considered through comparison of three peptides C ox LVINKLSQG, C ox LVINVLSQK, and C ox LVINVLSQR. Lastly, we rationalize the formation of b n-1 +H 2 O and a n-1 ions through a mechanism involving rearrangement of the C-terminal residue to form a mixed anhydride intermediate.

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High‐throughput method for on‐target performic acid oxidation of MALDI‐deposited samples

Cited by 7 publications

References 27 publications

Effect of Cysteic Acid Position on the Negative Ion Fragmentation of Proteolytic Derived Peptides

Effect of Cysteic Acid Position on the Negative Ion Fragmentation of Proteolytic Derived Peptides

Cycloquest: Identification of Cyclopeptides via Database Search of Their Mass Spectra against Genome Databases

Negative Ion Fragmentation of Cysteic Acid Containing Peptides: Cysteic Acid as a Fixed Negative Charge

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