Influence of temperature and crown ether complex formation on the charge partitioning between z and c fragments formed after electron capture by small peptide dications

Ehlerding, Anneli; Jensen, Camilla Skinnerup; Wyer, Jean Ann; Holm, Anne I. S.; Jørgensen, Palle E. T.; Kadhane, U.; Larsen, Mikkel Koefoed; Panja, Subhasis; Poully, Jean‐Christophe; Worm, E.; Zettergren, Henning; Hvelplund, P.; Nielsen, Steen Brøndsted

doi:10.1016/j.ijms.2009.01.019

Cited by 11 publications

(4 citation statements)

References 54 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Dissociation of mass-selected peptide ions is a basic technique for peptide sequencing and protein identification by means of mass spectrometric techniques. To drive the dissociation processes, excitation by multiple collisions with inert gas atoms (collision induced dissociation, CID 7 ) or surfaces (surface induced dissociation, SID 7 ), by electron capture (electron capture dissociation, ECD [8][9][10] ) and by blackbody infrared radiation 11,12 or laser light 13 has been employed. CID has been the most common method for peptide identification purposes.…”

Section: Introductionmentioning

confidence: 99%

Peptide fragmentation by keV ion-induced dissociation

Bari

Hoekstra

Schlathölter

2010

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

We have studied multiple ionization and dissociation of a trapped protonated peptide (leucine enkephalin) as induced by keV singly and doubly charged ions (H(+), He(+, 2+)) to demonstrate the potential of keV ions as a future tool for peptide identification. In contrast to conventional excitation techniques, the fragmentation pattern exhibits very strong peaks due to loss of sidechains in addition to those due to backbone scission. The results can be understood on the basis of the energy deposited into the peptide via electronic stopping. A pronounced dependence of the fragmentation pattern on the electronic structure of the projectile ions can be attributed to different electron capture efficiencies from localized molecular orbitals.

show abstract

Section: Introductionmentioning

confidence: 99%

Peptide fragmentation by keV ion-induced dissociation

Bari

Hoekstra

Schlathölter

2010

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

show abstract

“…Compared with the native peptide, the two peaks at m/z 489.45 and 505.18 are the singlyprotonated oxidation products with one or two oxygen atoms added, respectively, while the peaks at m/z 245. 22 and 253.13 are the doubly-protonated molecules of the above oxidation products [28]. Radiolysis also results in the loss of a guanidine group from the side chain of an Arg residue, giving rise to a characteristic product with a Ϫ43 Da mass change (peak at m/z 430.26 and 216.21) [25].…”

Section: Side-chain Oxidation Products Of Arramentioning

confidence: 99%

“…Here, we concentrated our work on small peptides that have few reaction channels, rendering the peaks in the spectra easy to assign [21][22][23]. Arginine-containing peptides provide a strong signal in positive ion ESI-MS and are often used as model peptides [24,25].…”

mentioning

confidence: 99%

The relative charge ratio between C and N atoms in amide bond acts as a key factor to determine peptide fragment efficiency in different charge states

Sun

Zong

Liu

et al. 2010

J. Am. Soc. Mass Spectrom.

View full text Add to dashboard Cite

The influence of charge state on the peptide dissociation behavior in tandem mass spectrometry (MS/MS) is worthy of discussion. Comparative studies of singly- and doubly-protonated peptide molecules are performed to explore the effect and mechanism of charge state on peptide fragmentation. In view of the charge-directed cleavage of protonated peptides described in the mobile proton model, radiolytic oxidation was applied to change the charge distribution of peptides but retain the sequence. Experimental studies of collision energy-dependent fragmentation efficiencies coupled with quantum chemical calculations indicated that the cleavage of ARRA and its side-chain oxidation products with oxygen atoms added followed a trend that doubly-protonated peptides fragment more easily than singly-protonated forms, while the oxidation product with the guanidine group deleted showed the opposite trend. By analyzing the charge distribution around the amide bonds, we found that the relative charge ratios between C and N atoms (Q(C)/Q(N)) in the amide bonds provided a reasonable explanation for peptide fragmentation efficiencies. An increase of the Q(C)/Q(N) value of the amide bond means that a peptide fragments more easily, and vice versa. The results described in this paper provide an experimental and calculation strategy for predicting peptide fragmentation efficiency.

show abstract

“…We have concentrated our work on small peptides, mainly dipeptides and tripeptides that can be made as doubly charged ions [30,38,39,41,52,53]. Such systems offer several advantages over larger peptides: there are few reaction channels, which renders the peaks in the spectra easy to assign.…”

mentioning

confidence: 99%

On the charge partitioning between c and z fragments formed after electron-capture induced dissociation of charge-tagged Lys-Lys and Ala-Lys dipeptide dications

Jensen

Holm

Zettergren

et al. 2009

J. Am. Soc. Mass Spectrom.

Self Cite

View full text Add to dashboard Cite

Here we report on the charge partition between c and z fragments formed after femtosecond collisional electron-transfer from Cs atoms to charge-tagged peptide dications. Peptides chosen for study were Ala-Lys (AK) and Lys-Lys (KK) where one or both of the lysine -amino groups were trimethylated to provide one or two fixed charges. For peptides with only one charge tag, the other charge was obtained by protonation of an amino group. In some experiments the ammonium group was tagged by 18-crown-6-ether (CE). Since recombination energies decrease in the order:, it is possible to change the probability for the transferred electron to end up at either the N-terminal or the C-terminal residue by CE attachment. We find, however, that the individual recombination energies have little influence on the relative ratio between the yield of c and z ions as long as there are no mobile protons that can be transferred between the two fragments. Our results can be accounted for by the Utah-Washington model where the electron is captured into an amide * orbital that weakens the N-C ␣ bond and causes its breakage, followed by proton, electron, or hydrogen transfer between the c and z fragments that stay together as an ion-molecule complex for some time. The data are also in accordance with the notion that an amide group competes with the charged groups for the electron. Electron capture by charged groups results in loss of small neutrals such as hydrogen and ammonia. (J Am Soc

show abstract

Influence of temperature and crown ether complex formation on the charge partitioning between z and c fragments formed after electron capture by small peptide dications

Cited by 11 publications

References 54 publications

Peptide fragmentation by keV ion-induced dissociation

Peptide fragmentation by keV ion-induced dissociation

The relative charge ratio between C and N atoms in amide bond acts as a key factor to determine peptide fragment efficiency in different charge states

On the charge partitioning between c and z fragments formed after electron-capture induced dissociation of charge-tagged Lys-Lys and Ala-Lys dipeptide dications

Contact Info

Product

Resources

About