An Unusual Family of Glycosylated Peptides Isolated from Dendroaspis angusticeps Venom and Characterized by Combination of Collision Induced and Electron Transfer Dissociation

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• 作者：Lo?c Quinton (1)
  Nicolas Gilles (2)
  Nicolas Smargiasso (1)
  Andrea Kiehne (3)
  Edwin De Pauw (1)
  
• 关键词：Venom ; Toxin ; Glycopeptide ; Electron transfer dissociation ; Dendroaspis angusticeps ; Peptide characterization ; Sequencing
• 刊名：Journal of The American Society for Mass Spectrometry
• 出版年：2011
• 出版时间：November 2011
• 年：2011
• 卷：22
• 期：11
• 页码：1891-1897
• 全文大小：480KB
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• 作者单位：Lo?c Quinton (1)
  Nicolas Gilles (2)
  Nicolas Smargiasso (1)
  Andrea Kiehne (3)
  Edwin De Pauw (1)
  
  1. Laboratoire de spectrométrie de masse, Département de Chimie-GIGA-R, Université de Liège, Liège, 4000, Belgium
  2. CEA, iBiTec-S, Service d’Ingénierie Moléculaire des Protéines (SIMOPRO), Gif sur Yvette, France
  3. Bruker Daltonik GmbH, Bremen, Germany
  

文摘

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. Second, 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.