A database of alkali metal-containing peptide cross sections: Influence of metals on size parameters for specific amino acids

Dilger, Jonathan M.; Valentine, Stephen J.; Glover, Matthew S.; Ewing, Michael A.; Clemmer, David E.

doi:10.1016/j.ijms.2012.05.001

Cited by 34 publications

(39 citation statements)

References 66 publications

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“…Figure 5 highlights that the substitution of a H + by a K + ion for a given charge state causes a reduction in CCS of the peptides independent of the presence of disulfide bonds in the peptide structure. This behavior can be correlated to a previous study [31], which demonstrates a sequence-dependent size reduction effect on linear peptides produced by a trypsin digest upon the substitution of protons by potassium cations. It should also be noted that no multiply potassiated species ( ,…) were found in the spectra of peptides bearing disulfide bonds, even when adding 100 μM KCl to the peptide solutions.…”

Section: Effect Of K + Adducts On Collision Cross-sectionssupporting

confidence: 88%

Ion Mobility-Mass Spectrometry as a Tool for the Structural Characterization of Peptides Bearing Intramolecular Disulfide Bond(s)

Massonnet

Haler

Upert

et al. 2016

J. Am. Soc. Mass Spectrom.

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Abstract. Disulfide bonds are post-translationnal modifications that can be crucial for the stability and the biological activities of natural peptides. Considering the importance of these disulfide bond-containing peptides, the development of new techniques in order to characterize these modifications is of great interest. For this purpose, collision cross cections (CCS) of a large data set of 118 peptides (displaying various sequences) bearing zero, one, two, or three disulfide bond(s) have been measured in this study at different charge states using ion mobility-mass spectrometry. From an experimental point of view, CCS differences (ΔCCS) between peptides bearing various numbers of disulfide bonds and peptides having no disulfide bonds have been calculated. The ΔCCS calculations have also been applied to peptides bearing two disulfide bonds but different cysteine connectivities (Cys1-Cys2/Cys3-Cys4; Cys1-Cys3/Cys2-Cys4; Cys1-Cys4/Cys2-Cys3). The effect of the replacement of a proton by a potassium adduct on a peptidic structure has also been investigated.

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Section: Effect Of K + Adducts On Collision Cross-sectionssupporting

confidence: 88%

Ion Mobility-Mass Spectrometry as a Tool for the Structural Characterization of Peptides Bearing Intramolecular Disulfide Bond(s)

Massonnet

Haler

Upert

et al. 2016

J. Am. Soc. Mass Spectrom.

View full text Add to dashboard Cite

show abstract

“…In fact, there are only three individual studies which have reported over 1,000 CCS values and thus would be considered large-scale surveys, 54,55,72 underscoring the fact that the reporting of quantitative ion mobility measurements is predominantly an interlaboratory initiative.…”

Section: Significant Ccs Contributionsmentioning

confidence: 99%

Ion Mobility Collision Cross Section Compendium

2016

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In this review, we focus on an important aspect of ion mobility (IM) research, namely the reporting of quantitative ion mobility measurements in the form of the gas-phase collision cross section (CCS), which has provided a common basis for comparison across different instrument platforms and offers a unique form of structural information, namely size and shape preferences of analytes in the absence of bulk solvent. This review surveys the over 24,000 CCS values reported from IM methods spanning the era between 1975 to 2015, which provides both a historical and analytical context for the contributions made thus far, as well as insight into the future directions that quantitative ion mobility measurements will have in the analytical sciences. The analysis was conducted in 2016, so CCS values reported in that year are purposely omitted. In another few years, a review of this scope will be intractable, as the number of CCS values which will be reported in the next three to five years is expected to exceed the total amount currently published in the literature.

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“…In addition, ISPs provide general insight into peptide structure. For example, Dilger et al calculated ISPs for alkali-and alkaline-earth-coordinated peptides to gain insight into the interactions between metal cations and specific amino acid residues that influence peptide ion structure [43, 44]. ISPs were recently extended to PTMs with palmitoylated peptides [45].…”

Section: Introductionmentioning

confidence: 99%

Examining the Influence of Phosphorylation on Peptide Ion Structure by Ion Mobility Spectrometry-Mass Spectrometry

Glover

Dilger

Acton

et al. 2016

J. Am. Soc. Mass Spectrom.

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Ion mobility spectrometry-mass spectrometry (IMS-MS) techniques are used to study the general effects of phosphorylation on peptide structure. Cross sections for a library of 66 singly phosphorylated peptide ions from 33 pairs of positional isomers, and unmodified analogues were measured. Intrinsic size parameters (ISPs) derived from these measurements yield calculated collision cross sections for 85% of these phosphopeptide sequences that are within ±2.5% of experimental values. The average ISP for the phosphoryl group (0.64 ± 0.05) suggests that in general this moiety forms intramolecular interactions with the neighboring residues and peptide backbone, resulting in relatively compact structures. We assess the capability of ion mobility to separate positional isomers (i.e., peptide sequences that differ only in the location of the modification) and find that more than half of the isomeric pairs have >1% difference in collision cross section. Phosphorylation is also found to influence populations of structures that differ in the cis/trans orientation of Xaa–Pro peptide bonds. Several sequences with phosphorylated Ser or Thr residues located N-terminally adjacent to Pro residues show fewer conformations compared to the unmodified sequences.

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A database of alkali metal-containing peptide cross sections: Influence of metals on size parameters for specific amino acids

Cited by 34 publications

References 66 publications

Ion Mobility-Mass Spectrometry as a Tool for the Structural Characterization of Peptides Bearing Intramolecular Disulfide Bond(s)

Ion Mobility-Mass Spectrometry as a Tool for the Structural Characterization of Peptides Bearing Intramolecular Disulfide Bond(s)

Ion Mobility Collision Cross Section Compendium

Examining the Influence of Phosphorylation on Peptide Ion Structure by Ion Mobility Spectrometry-Mass Spectrometry

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