Influence of salt bridge interactions on the gas-phase stability of DNA/peptide complexes

Alvès, Sandra; Woods, Amina S.; Delvolvé, Alice; Tabet, Jean Claude

doi:10.1016/j.ijms.2008.04.023

Cited by 19 publications

(28 citation statements)

References 58 publications

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“… It is also noteworthy that the [BDSA‐H] − signal following CID, which arises from detachment of the reagent from the complex as a singly charged species due to proton transfer, is quite small, and essentially no evidence for loss of neutral BDSA is observed. This confirms that cleavage of covalent bonds can be highly competitive with loss of the non‐covalently bound BDSA …”

Section: Resultssupporting

confidence: 63%

“…This confirms that cleavage of covalent bonds can be highly competitive with loss of the non-covalently bound BDSA. [37][38][39] The angiotensin II data support the hypothesis that the [M + ♦] À species formed from the dehydration of the [angiotensin II + FBDSA] À adduct is comprised of a mixture of structures. While the nominal structure of the Schiff base product is clear (i.e.…”

Section: Mass Spectrometrysupporting

confidence: 55%

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Covalent and non‐covalent binding in the ion/ion charge inversion of peptide cations with benzene‐disulfonic acid anions

2012

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Protonated angiotensin II and protonated leucine enkephalin-based peptides, which included YGGFL, YGGFLF, YGGFLH, YGGFLK, and YGGFLR, were subjected to ion/ion reactions with the doubly deprotonated reagents 4-formyl-1,3-benzenedisulfonic acid (FBDSA) and 1,3-benzenedisulfonic acid (BDSA). The major product of the ion/ion reaction is a negatively charged complex of the peptide and reagent. Following dehydration of [M+FBDSA-H]− via collisional induced dissociation (CID), angiotensin II (DRVYIHPF) showed evidence for two product populations, one in which a covalent modification has taken place and one in which an electrostatic modification has occurred (i.e., no covalent bond formation). A series of studies with model systems confirmed that strong non-covalent binding of the FBDSA reagent can occur with subsequent ion trap CID resulting in dehydration unrelated to the adduct. Ion trap CID of the dehydration product can result in cleavage of amide bonds in competition with loss of the FBDSA adduct. This scenario is most likely for electrostatically-bound complexes in which the peptide contains both an arginine residue and one or more carboxyl groups. Otherwise, loss of the reagent species from the complex, either as an anion or as a neutral species, is the dominant process for electrostatically-bound complexes. The results reported here shed new light on the nature of non-covalent interactions in gas-phase complexes of peptide ions that can be used in the rationale design of reagent ions for specific ion/ion reaction applications.

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Section: Resultssupporting

confidence: 63%

Section: Mass Spectrometrysupporting

confidence: 55%

Covalent and non‐covalent binding in the ion/ion charge inversion of peptide cations with benzene‐disulfonic acid anions

2012

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“…Supplemental Figure S3 summarizes relationships between charge state, ion pairs, and dissociation pathways. Preferential covalent bond cleavage has also been noted for noncovalent complexes between DNA and basic peptides [96], where electrostatic interactions are also important.…”

Section: How Symmetric and Asymmetric Dissociations Differmentioning

confidence: 99%

Salt Bridge Rearrangement (SaBRe) Explains the Dissociation Behavior of Noncovalent Complexes

Loo

2016

J. Am. Soc. Mass Spectrom.

119

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Native electrospray ionization-mass spectrometry, with gas phase activation and solution compositions that partially release subcomplexes, can elucidate topologies of macromolecular assemblies. That so much complexity can be preserved in gas phase assemblies is remarkable, although a long-standing conundrum has been the differences between their gas and solution phase decompositions. Collision-induced dissociation of multimeric noncovalent complexes typically distributes products asymmetrically; i.e., by ejecting a single subunit bearing a large percentage of the excess charge. That unexpected behavior has been rationalized as one subunit “unfolding” to depart with more charge. We present an alternative explanation based on heterolytic ion-pair scission and rearrangement, X-COO−…H3+N-Y→X-COO−+H3+N-Y a mechanism that inherently partitions charge asymmetrically. Excessive barriers to dissociation are circumvented in this manner, when local charge rearrangements access a lower-barrier surface. An implication of this ion pair consideration is that stability differences between high- and low-charge state ions usually attributed to Coulomb repulsion may, alternatively, be conveyed by attractive forces from ion pairs (salt bridges) stabilizing low-charge state ions. Should the number of ion pairs be roughly inversely related to charge, symmetric dissociations would be favored from highly charged complexes, as observed. Correlations between a gas phase protein’s size and charge reflect the quantity of restraining ion pairs. Collisionally-facilitated salt bridge rearrangement (SaBRe) may explain unusual size “contractions” seen for some activated, low charge state complexes. That some low-charged multimers preferentially cleave covalent bonds or shed small ions to disrupting noncovalent associations is also explained by greater ion pairing in low charge state complexes.

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“…This means that one zwitterion or several zwitterions (according to the strand size) already described in MALDI must coexist with the corresponding canonical form . Such zwitterions were currently considered rather than their corresponding canonical forms to explain dissociations of multiply charged species generated in electrospray . Consequently, formation of [M–H] − may take place from desorbed excited aggregates by neutralization of one positive charge in several zwitterions and/or by releasing one proton from one of its neutral sites (or from the canonical form).…”

Section: Discussionmentioning

confidence: 99%

“…[25] Such zwitterions were currently considered rather than their corresponding canonical forms to explain dissociations of multiply charged species generated in electrospray. [12,35] Consequently, formation of [M-H] À may take place from desorbed excited aggregates by neutralization of one positive charge in several zwitterions and/or by releasing one proton from one of its neutral sites (or from the canonical form). The zwitterion production in the gas phase requires presence of highly basic site(s) as well as highly acidic site(s).…”

Section: Analysis Of Deprotonated Rna/dna Chimerasmentioning

confidence: 99%

A revisit of high collision energy effects on collision‐induced dissociation spectra using matrix‐assisted laser desorption/ionization tandem time‐of‐flight mass spectrometry (MALDI‐LIFT‐TOF/TOF): application to the sequencing of RNA/DNA chimeras

Mauger

Tabet

Gut

2014

Rapid Comm Mass Spectrometry

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Influence of salt bridge interactions on the gas-phase stability of DNA/peptide complexes

Cited by 19 publications

References 58 publications

Covalent and non‐covalent binding in the ion/ion charge inversion of peptide cations with benzene‐disulfonic acid anions

Covalent and non‐covalent binding in the ion/ion charge inversion of peptide cations with benzene‐disulfonic acid anions

Salt Bridge Rearrangement (SaBRe) Explains the Dissociation Behavior of Noncovalent Complexes

A revisit of high collision energy effects on collision‐induced dissociation spectra using matrix‐assisted laser desorption/ionization tandem time‐of‐flight mass spectrometry (MALDI‐LIFT‐TOF/TOF): application to the sequencing of RNA/DNA chimeras

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