Insights into the fragmentation pathways of gas-phase protonated sulfoserine

Patrick, Amanda L.; Stedwell, Corey N.; Schindler, Baptiste; Compagnon, Isabelle; Berden, Giel; Oomens, Jos; Polfer, Nicolas C.

doi:10.1016/j.ijms.2014.12.001

Cited by 21 publications

(43 citation statements)

References 42 publications

(49 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Thus, observed interaction in SAALsSLLR peptide can be attributed to the secondary structure stabilisation via hydrogen bonds. Upon SO 3 abstraction from the sulfonated side chain, the side chain residue takes the form structurally analogous to the unmodified hydroxylcontaining residue, consistent with the IRMPD observations on sulfoserine [18]. At this point, SO 3 molecule probably interacts with peptide and consequently the ion-molecule complex dissociates making the neutral loss of SO 3 a two-step process (abstraction and ion-molecule complex dissociation), in accordance with observations of phosphopeptides dissociation dynamics [26].…”

Section: Cid Of Sulfonated Peptides -Mobile Proton Environmentsupporting

confidence: 87%

“…The mechanism is similar to the one associated with the loss of metaphosphoric acid in phosphorylated peptides [7] and was hypothesised for the sulfo group loss from sulfoserine [18].…”

Section: Cid Of Sulfonated Peptides -Mobile Proton Environmentmentioning

confidence: 55%

“…Understanding of the gas-phase dissociation pathways of sulfonated peptides is very limited. Recently, Patrick et al preformed structural investigation of protonated sulfoserine dissociation pathways [18]. Low-energy CID of protonated sulfoserine produced two major product ions: 3-member aziridine ring structure attributed to the neutral loss of 98 Da (loss of H 2 SO 4 ) and a structure identical to the protonated serine was related to the loss of 80 Da (loss of SO 3 ).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Study of the gas-phase fragmentation behaviour of sulfonated peptides

Škulj

Rožman

2015

International Journal of Mass Spectrometry

View full text Add to dashboard Cite

a b s t r a c tA series of singly and doubly protonated peptides bearing sulfonated residue have been studied, using both experiment and molecular modelling, to elucidate fragmentation chemistry of sulfonated peptides. Collision-induced dissociation mass spectra indicate that the sulfo group loss (neutral loss of 80 Da) is the dominant dissociation channel. Modelling results suggest the proton transfer mechanism, where upon vibrational excitation, the acidic side chain proton is transferred from the sulfo group hydroxyl to the ester oxygen resulting in S O bond cleavage and formation of the unmodified hydroxyl containing residue and SO 3 . Conformations associated with potential energy profile of the reaction imply the charge remote nature of the proposed mechanism. The proposed proton transfer mechanism was compared with the intramolecular nucleophilic substitution (S N 2) mechanism, the main pathway suggested for neutral loss of phosphoric acid from phosphopeptides. Both pathways (proton transfer and S N 2) are available for sulfonated and phosphorylated peptides; however, each posttranslational modification favours different mechanism. The change of the bond dissociation enthalpies and the ability of stabilising the transition state structures are demonstrated as main factors responsible for each posttranslational modification activating a different pathway.

show abstract

Section: Cid Of Sulfonated Peptides -Mobile Proton Environmentsupporting

confidence: 87%

“…The mechanism is similar to the one associated with the loss of metaphosphoric acid in phosphorylated peptides [7] and was hypothesised for the sulfo group loss from sulfoserine [18].…”

Section: Cid Of Sulfonated Peptides -Mobile Proton Environmentmentioning

confidence: 55%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Study of the gas-phase fragmentation behaviour of sulfonated peptides

Škulj

Rožman

2015

International Journal of Mass Spectrometry

View full text Add to dashboard Cite

show abstract

“…Structures of the product ions were determined using a combination of mass spectrometry, infrared multiple photon dissociation (IRMPD) spectroscopy and theoretical calculations. IRMPD spectroscopy has previously been used to determine the structures of several protonated peptide precursor ions and fragments [17][18][19][20][21][22], and has proven to be a powerful method to distinguish isomers, (prototropic) tautomers and conformers [18,21,[23][24][25][26][27][28][29][30][31][32][33].…”

Section: Introductionmentioning

confidence: 99%

Dehydration reactions of protonated dipeptides containing asparagine or glutamine investigated by infrared ion spectroscopy

Kempkes

Martens

Berden

2018

International Journal of Mass Spectrometry

Self Cite

View full text Add to dashboard Cite

The role of specific amino acid side-chains in the fragmentation chemistry of gaseous protonated peptides resulting from collisional activation remains incompletely understood. For small peptides containing asparagine and glutamine, a dominant fragmentation channel induced by collisional activations is, in addition to deamidation, the loss of neutral water. Identifying the product ion structures from H2O-loss from four protonated dipeptides containing Asn or Gln using infrared ion spectroscopy, mechanistic details of the dissociation reactions are revealed. Several sequential dissociation reactions have also been investigated and provide additional insights into the fragmentation chemistry. While water loss can in principle occur from the C-terminus, the side chain or the amide bond carbonyl oxygen, in most cases the C-terminus was found to detach H2O, leading to a b2-sequence ion with an oxazolone structure for AlaGln, and bifurcating mechanisms leading to both oxazolone and diketopiperazine species for AlaAsn and AsnAla. In contrast, GlnAla expels water from the amide side chain leading to an imino-substituted prolinyl structure.

show abstract

“…Ion spectroscopy is a proven tool for establishing the molecular structures of gas-phase amino acid ions, [19] their (de)protonation sites, [20][21][22] and the structures of their gasphase reaction products in collision-induced dissociation (CID) tandem mass spectrometry (MS/MS). [23] Here, the fragmentation reactions after CID of AsnH + and GlnH + are investigated using ion spectroscopy. Computed spectra for previously established or suggested isomers [12,13] are therefore compared with the measured IRMPD spectra.…”

mentioning

confidence: 99%

Deamidation reactions of protonated asparagine and glutamine investigated by ion spectroscopy

Kempkes

Martens

Grzetic

et al. 2016

Rapid Comm Mass Spectrometry

Self Cite

View full text Add to dashboard Cite

RATIONALE:Deamidation of Asn and Gln residues is a primary route for spontaneous posttranslational protein modification. Various structures have been proposed for the deamidation products of the protonated amino acids. Here we verify these structures by ion spectroscopy, as well as the structures of parallel and sequential fragmentation products. METHODS:Infrared ion spectroscopy using the free electron laser FELIX has been applied to the reaction products from deamidation of protonated glutamine and asparagine in a tandem mass spectrometer. IR spectra were recorded over the 800-1900 cm -1 spectral range by infrared multiple-photon dissociation (IRMPD) spectroscopy. Molecular structures of the fragment ions are derived from comparison of the experimental spectra with spectra predicted for different candidate structures by density functional theory (DFT) calculations. RESULTS:[AsnH + -NH 3 ] + is found to possess a 3-amino succinic anhydride structure protonated on the amino group. The dissociation reaction involving loss of H 2 O and CO forms a linear immonium ion. For [GlnH + -NH 3 ] + , the N-terminal nitrogen acts as the nucleophile leading to an oxo-proline product ion structure. For [GlnH + -NH 3 ] + a sequential loss of [CO + H 2 O] is found, leading to a pyrolidone-like structure. We also confirm by IR spectroscopy that dehydration of protonated aspartic acid (AspH + ) and glutamic acid (GluH + ) leads to identical structures as to those found for the loss of NH 3 from AsnH + and GlnH + .2 CONCLUSIONS: The structure determined for AsnH + is in agreement with the suggested structure derived from measured and computed activation energies. Infrared ion spectra for the NH 3 -loss product from GlnH + establish that a different reaction mechanism occurs for this species as compared to AsnH + . For both amino acids, loss of NH 3 occurs from the side-chain.

show abstract

Insights into the fragmentation pathways of gas-phase protonated sulfoserine

Cited by 21 publications

References 42 publications

Study of the gas-phase fragmentation behaviour of sulfonated peptides

Study of the gas-phase fragmentation behaviour of sulfonated peptides

Dehydration reactions of protonated dipeptides containing asparagine or glutamine investigated by infrared ion spectroscopy

Deamidation reactions of protonated asparagine and glutamine investigated by ion spectroscopy

Contact Info

Product

Resources

About