Reference : Attribution of Cysteine Connectivities in small toxins - New Prospects Based on Parti...
Scientific congresses and symposiums : Unpublished conference/Abstract
Physical, chemical, mathematical & earth Sciences : Chemistry
http://hdl.handle.net/2268/164150
Attribution of Cysteine Connectivities in small toxins - New Prospects Based on Partial Oxidation/Reduction Experiments and Ion-Mobility Mass Spectrometry
English
Quinton, Loïc mailto [Université de Liège - ULiège > Département de chimie (sciences) > Chimie biologique >]
Massonnet, Philippe mailto [Université de Liège - ULiège > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.) >]
Echterbille, Julien mailto [Université de Liège - ULiège > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.) >]
Degueldre, Michel mailto [Université de Liège - ULiège > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.) >]
Smargiasso, Nicolas mailto [Université de Liège - ULiège > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.) >]
Gilles, Nicolas []
Upert, Gregory []
Pastor, Alexandra []
De Pauw, Edwin mailto [Université de Liège - ULiège > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.) >]
Dec-2013
Yes
Yes
21st Meeting of the French Society for Toxinology: “Fresh water and Marine Toxins”
décembre 2013
[en] venomics ; ion-mobility ; mass-spectrometry
[en] Disulfide bonds are post-translational modifications often found in biological compounds and especially in animal toxins. Disulfide bonds participate in the formation of specific folding of peptides and proteins, directly related to their biological activity.

Cystein pairing determinations are primordial for the synthesis of chemical homologous displaying the same bioactivity than the natural compound. This task appears already difficult when the cysteine pairings have to be determined from large proteins. The combination of physical and chemical techniques such as NMR, enzymatic proteolysis, liquid chromatography and mass spectrometry, is needed to circumvent this difficulty. However, when the work concerns small compounds such as conotoxins, the problem is much more complex due to the low amount of available compound and to the lack of enzymatic cleavage sites between cysteines.

In this study, we investigate the case of small peptides that contain two disulphide bonds. The idea is to determine the cystein pairings in such compounds by a chemical partial reduction (or oxidation) of the peptides, followed by the separation of the generated species by ion-mobility mass spectrometry, and their characterisation by tandem mass spectrometry. Up to now, we have investigated the partial reduction not only in solution (with DTT and TCEP) but also in the gas-phase (Electron transfer dissociation), and partial oxidation in solution (with 3-CPBA). The results demonstrate an unexpected complexity of the data, including low fragmentation ratios of peptides and disulfide scramblings.
Researchers ; Professionals ; Students
http://hdl.handle.net/2268/164150

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