Reference : An Unusual Family of Glycosylated Peptides Isolated from Dendroaspis angusticeps Venom a...
Scientific journals : Article
Physical, chemical, mathematical & earth Sciences : Chemistry
http://hdl.handle.net/2268/108029
An Unusual Family of Glycosylated Peptides Isolated from Dendroaspis angusticeps Venom and Characterized by Combination of Collision Induced and Electron Transfer Dissociation
English
Quinton, Loïc mailto [Université de Liège - ULg > Département de chimie (sciences) > Chimie biologique >]
Gilles, Nicolas mailto [Commissariat à l'Energie Atomique (Saclay) - CEA > ibitech-SiMoPro > > >]
Smargiasso, Nicolas mailto [Université de Liège - ULg > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.) >]
Kiehne, Andrea mailto [Bruker Daltonik GmbH > > > >]
De Pauw, Edwin mailto [Université de Liège - ULg > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.) >]
Nov-2011
Journal of the American Society for Mass Spectrometry
Elsevier Science
22
11
1891-1897
Yes (verified by ORBi)
International
1044-0305
New York
NY
[en] Venomics ; Toxin ; Peptide ; Structure ; Sequencing ; Glycosylation
[en] This study describes the structural characterization of a totally new family of peptides from the venom of the snake green mamba (Dendroaspis angusticeps). Interestingly, these peptides differ in several points from other already known mamba toxins. First of all, they exhibit very small molecular masses, ranging from 1.3 to 2.4 kDa. The molecular mass of classical mamba toxins is in the range of 7 to 25 kDa. Secondly, the new peptides do not contain disulfide bonds, a post-translational modification commonly encountered in animal toxins. The third difference is the very high proportion of proline residues in the sequence accounting for about one third of the sequence. Finally, these new peptides reveal a carbohydrate moiety, indicating a glycosylation in the sequence. The last two features have made the structural characterization of the new peptides by mass spectrometry a real analytical challenge. Peptides were characterized by a combined use of MALDI- TOF/TOF and nanoESI-IT-ETD experiments to determine not only the peptide sequence but also the composition and the position of the carbohydrate moiety. Anyway, such small glycosylated and proline-rich toxins are totally different from any other known snake peptide and form, as a consequence, a new family of peptides.
Researchers ; Professionals ; Students
http://hdl.handle.net/2268/108029
10.1007/s13361-011-0210-0
http://www.springerlink.com/content/0253266161k6vh17/

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