Max Goyffon
University of Orléans
18 Papers
219 Citations
Max Goyffon is an academic researcher from University of Orléans. The author has contributed to research in topics: Androctonus australis & Fusion protein. The author has an hindex of 10, co-authored 18 publications.
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Papers
A recombinant single-chain antibody fragment that neutralizes toxin II from the venom of the scorpion Androctonus australis hector
TL;DR: This work neutralized the pharmacological and biological properties of a scorpion neurotoxin with a single‐chain Fv, which opens new perspectives for the treatment of envenomizations.
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Construction and functional evaluation of a single-chain antibody fragment that neutralizes toxin AahI from the venom of the scorpion Androctonus australis hector.
TL;DR: A recombinant scFv is produced that reproduces the recognition properties of the parent antibody and neutralizes the scorpion neurotoxin AahI, thereby opening new prospects for the treatment of envenomation.
Design and evaluation of a diabody to improve protection against a potent scorpion neurotoxin.
Nicolas Aubrey,Christiane Devaux,Pierre Yves Sizaret,Hervé Rochat,Max Goyffon,Philippe Billiald +5 more
TL;DR: In this article, a diabody derived from monoclonal antibody 9C2 was used to neutralize the toxicity of scorpion neurotoxin AahI in mammals.
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Engineering of a recombinant Fab from a neutralizing IgG directed against scorpion neurotoxin AahI, and functional evaluation versus other antibody fragments
Nicolas Aubrey,Julien Muzard,Jean Péter,Hervé Rochat,Max Goyffon,Christiane Devaux,Philippe Billiald +6 more
TL;DR: The antibody engineering approach presented here provides an innovative way to synthesize novel toxin-neutralizing molecules and may serve as a strategy for designing a new generation of antivenoms.
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Peptide profiling by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry of the Lasiodora parahybana tarantula venom gland.
TL;DR: In situ MALDI analysis of L. parahybana venom gland sections revealed different peptide expression levels all along the gland and non-processed peptide precursors, demonstrating the power of the method for the dynamic investigation of peptide evolution in the venom gland of spiders.
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