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Gervaise MOSSER Equipe Matériaux du Vivant Laboratoire de Chimie de la Matière Condensée de Paris UMR 7574-CNRS/UPMC/ENSCP/Collège de France/EPHE 4 Place Jussieu, 75005 PARIS, France. [email protected] Tel : 00.33.(0)1.4427.6553 Fax : 00.33.(0)1.4427.6539

The collagen I molecule is composed of three polypeptide chains of about 1000 amino-acids each structured in a left handed helix, the three of them forming a right handed super helix. It is the major structural protein of the body and is found organised in a hierarchical manner in the extra-cellular matrix of many tissues (skin [1], bone [2], tendon [3], cornea and sclera [4], etc..) It is the fundamental brick responsible for their long-range specific architecture and the physical properties required for their function (elasticity, resistance, transparency etc..). Thus we find a random organization in skin, helicoidal in bone, crimp in tendon, plywood helicoidal in sclera and cornea. In-vivo, collagen I is found in cross-striated fibrils associated with other molecules. The fibrils are described forming fibres which themselves form larger entities called fascicles. The long-range organization described above is observed in histological sections at the millimetre sub-level. In our group, we try to identify the different physical parameters that can influence both the long range and the hierarchical organization of collagen in vitro. The goals are first to synthesize dense collagen matrices that would mimic the living tissues for medical applications and cell culture support and, second, to understand better in vivo tissue morphogenesis processes. We have evidenced the role of collagen I and acid acetic concentrations, pH and ionic force on the structural properties of collagen I solutions and/or on the sol-gel transition that lead to dense collagen matrices [5,6,7,8]. [1] L.C.U. Junqueria, G.S. Montes, J.E.C. Martins, P.P. Joazeiro. Histochemistry, 79, (1983). [2] M.M. Giraud-Guille. Calcif. Tissue. Int., 42 (1988). [3] J. Dlugosz, L.J. Gathercole, A. Keller. Micron, 9, (1978). [4] A.J. Coulombre. Adv. Morphog. 4 (1965). [5] M.M. Giraud-Guille. Mole. Cryst. Liq. Cryst., 153, (1988). [6] G. Mosser, A. Anglo, C. Helary, Y. Bouligand, M.M. Giraud-Guille, Matrix Biol. 25 (2006). [7] F. Gobeaux, G. Mosser, A. Anglo, P. Panine, P. Davidson, M.M. Giraud-Guille, E. Belamie, J . Mol. Biol., 376, (2008). [8] F. Gobeaux, E. Belamie, G. Mosser, P. Davidson, P. Panine, M.M. Giraud-Guille. Langmuir, 23, (2007).

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Gervaise MOSSER

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