Reference : Venomics: unravelling the complexity of animal venoms with mass spectrometry
Scientific journals : Article
Physical, chemical, mathematical & earth Sciences : Chemistry
http://hdl.handle.net/2268/10067
Venomics: unravelling the complexity of animal venoms with mass spectrometry
English
Escoubas, Pierre mailto [Université de Nice-Sophia Antipolis > Institut de pharmacologie moléculaire et cellulaire > CNRS-UMR6097 > >]
Quinton, Loïc mailto [Université de Liège - ULg > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.) > >]
Nicholson, Graham M. mailto [University of Technology Sydney > Neurotoxin research group > Departement of Medical and Molecular Biosciences > >]
2008
Journal of Mass Spectrometry [=JMS]
John Wiley & Sons, Inc
43
279-295
Yes (verified by ORBi)
International
1076-5174
Chichester
United Kingdom
[en] Venomics ; Mass spectrometry ; Toxin
Giga-Systems Biology and Chemical Biology
Researchers ; Professionals ; Students
http://hdl.handle.net/2268/10067
10.1002/jms.1389
http://www.interscience.wiley.com
Animal venoms and toxins are now recognized as major sources of bioactive molecules that my be tomorrow’s new drug leads. Their complexity and their potential as drugs sources have been demonstrated by application of modern analytical technologies, which have revealed venoms to be vast peptide combinatorial libraries. Structural as well as pharmacological diversity is immense, and mass spectrometry is now one of the major investigative tool for the structural investigation of venom components. Recent advances in its use in the study of venom and toxins are reviewed. The application of mass spectrometry techniques to peptide toxin sequence determination by de novo sequencing is discussed in detail, in the light of the search for novel analgesic drugs. We also present the combined application of LC-MALDI separation with mass fingerprinting and ISD fragmentation for the determination of structural and pharmacological classes of peptides in complex spider venoms. This approach now serves as the basis for the full investigation of complex spider venom proteomes, in combination with cDNA analysis.

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