De la difficulté à valoriser les résultats de la recherche

Depuis quelques années, une petite révolution est en route au CNRS avec l’apparition du chercheur/entrepreneur. Ce chef d’entreprise d’un genre nouveau contribue à changer le visage de la recherche fondamentale en la propulsant dans le monde de l’innovation et de l’économie. Bernard Pau, ancien responsable du département des sciences de la vie du CNRS (SDV), nous livre son point de vue.In addition to the conventional public-private R&D partnerships, a radical change in the industry transfer of innovations from academic research has taken place at CNRS a few years ago with the creation of biotech companies as spin off from laboratories. Bernard Pau, former director of the Life Sciences Department at CNRS, gives us some comments about opportunities and difficulties in this field

Systematic mapping of regions of human cardiac troponin I involved in binding to cardiac troponin C: N- and C-terminal low affinity contributing regions

AbstractThe Spot method of multiple peptide synthesis was used to map in a systematic manner regions of the human cardiac troponin I sequence (hcTnI) involved in interactions with its physiological partner, troponin C (cTnC). Ninety-six 20-mer peptides describing the entire hcTnI sequence were chemically assembled; their reactivity with [125I]cTnC, in the presence of 3 mM Ca2+, enabled the assignment of six sites of interaction (residues 19–32, 45–54, 129–138, 145–164, 161–178 and 191–210). For several sites, a good correlation with literature data was obtained, thus validating this methodological approach. Synthetic peptides, each containing in their sequence an interaction site, were prepared. As assessed by BIACORE, all of them exhibited an affinity for cTnC in the range of 10−6–10−7 M, except for hcTnI [39–58] which showed a nanomolar affinity. This peptide was also able to block the interaction between hcTnI and cTnC. We therefore postulate that despite the existence of multiple cTnC interaction sites on the hcTnI molecule, only that region of hcTnI allows a stabilization of the complex. Residues 19–32 from the N-terminal cardio-specific extension of hcTnI were also found to be involved in interaction with cTnC; residues 19–32 may correspond to the minimal sequence of the extension which could switch between the N- and C-terminal TnC domains, depending on its phosphorylation state. Finally, two Ca2+-dependent cTnC binding domains within the C-terminal part of hcTnI (residues 164–178 and 191–210) were also mapped. The latter site may be linked with the cardiac dysfunction observed in stunned myocardium

Low-frequency gravitational-wave science with eLISA/NGO

We review the expected science performance of the New Gravitational-Wave Observatory (NGO, a.k.a. eLISA), a mission under study by the European Space Agency for launch in the early 2020s. eLISA will survey the low-frequency gravitational-wave sky (from 0.1 mHz to 1 Hz), detecting and characterizing a broad variety of systems and events throughout the Universe, including the coalescences of massive black holes brought together by galaxy mergers; the inspirals of stellar-mass black holes and compact stars into central galactic black holes; several millions of ultracompact binaries, both detached and mass transferring, in the Galaxy; and possibly unforeseen sources such as the relic gravitational-wave radiation from the early Universe. eLISA's high signal-to-noise measurements will provide new insight into the structure and history of the Universe, and they will test general relativity in its strong-field dynamical regime.Comment: 20 pages, 8 figures, proceedings of the 9th Amaldi Conference on Gravitational Waves. Final journal version. For a longer exposition of the eLISA science case, see http://arxiv.org/abs/1201.362