Current status : Senior Scientist (Directeur de Recherche INSERM)
Institution: Université de la Méditerranée et Université Paul Cézanne, CNRS UMR 6231, CNR2M, ToxCIM team, Faculté de Médecine Nord, Institut Fédératif Jean Roche INSERM/CNRS/APHM/ Bd Pierre Dramard, 13326, Marseille, Cedex 15, France. Directeur: Pr. Alain Enjalbert
-Doctorat de 3 ème cycle en Biochimie Cellulaire et Moléculaire (1981). Faculté des Sciences de Luminy, University Aix-Marseilles II, Marseilles.
-Doctorat d'Etat ès Sciences Physiques (1987). Faculté des Sciences de Luminy, University Aix-Marseilles II, Marseilles.
-Height months at the “Institut Ezequiel Diaz” and at the “Federal University of Minas-Gerais”, Belo-Horizonte, Brazil (Grants INSERM/CNPq and CAPES/COFECUB).
-Sabbatical year at the Carlsberg Institute, Copenhagen, Denmark (Grant from the European Community, BRIDGE program).
- Vice-President of the French Society of Toxinology (SFET) during 10 years (until 2006) and now member of its board
- Member of the International Society of Toxinology (IST)
Total of Original publications (2010):
99 under the name of Martin-Eauclaire MF and 20 under the name of Martin MF
My main scientific interest is about scorpion venoms and their toxins. I focused my fundamental studies on the structure-function relationships of the toxins and their targets in order to solve the question of their respective selectivity. I have purified and chemically and pharmacologically characterized more than fifty new molecules active on voltage-gated sodium channels (VGSCs) or on potassium channels. The most well known are the potent beta-type toxins from Centruroides suffusus suffusus (as Css II, CssIV and Css VI), which allowed the site four definition on VGSCs, and Kaliotoxin (KTX), a high affinity and quite selective blocker of the potassium channel Kv1.3. KTX led to the first 3D-structure resolution, using solid-state NMR spectroscopy, of the interface between a “short” scorpion toxin and a potassium channel. It was shown that conformational changes of both the toxin and the channel were crucial for the tight interaction (collaboration with the ZMNH, Hamburg and the Max Planck Institute, Göttingen, Germany). More recently, I have been involved in the definition of the scorpion alpha and beta-type toxins binding sites (known as sites three and four) on the so-called “paddle-motifs” from the four domains of neuronal and muscular sodium VGSCs (Nav1.2 and Nav1.4 respectively) shifted with those of the potassium channel Kv2.1 (collaboration with scientists from the NIH, Bethesda, USA).