| AVS 55th International Symposium & Exhibition | |
| Biomaterial Interfaces | Monday Sessions |
| Session BI+SS+NC-MoA |
| Session: | Honorary Session for Bengt Kasemo |
| Presenter: | A.R. Brisson, CNRS-University of Bordeaux, France |
| Authors: | A.R. Brisson, CNRS-University of Bordeaux, France N. Arraud, CNRS-University of Bordeaux, France R. Bérat, CNRS-University of Bordeaux, France A. Bouter, CNRS-University of Bordeaux, France B. Garnier, CNRS-University of Bordeaux, France C. Gounou, CNRS-University of Bordeaux, France J. Lai-Kee-Him, CNRS-University of Bordeaux, France S. Tan, CNRS-University of Bordeaux, France |
| Correspondent: | Click to Email |
The self-assembly of proteins in 2D arrays at membrane surfaces is a generic strategy used by the cell for the construction of functional supramolecular edifices, e.g. bacterial S-layers, inter-membrane cadherin junctions, etc.. Annexin-A5 (Anx5) is the prototype member of the annexins, a superfamily proteins which share the properties of binding to negatively charged phospholipids in the presence of Ca2+ ions and forming various types of 2D ordered arrays at membrane surfaces. A detailed model of the structure and mechanism of formation of Anx5 2D arrays has been elaborated from EM, AFM and physico-chemical studies on various types of model membranes – liposomes in solution, lipid monolayers at the air-water interface, supported lipid bilayers.1-4 The long-debated question of the functional role of Anx5 and annexins starts to be elucidated. The unique properties of binding and 2D self-assembly of Anx5 were exploited to develop various types of molecular tools for nanobiotechnological applications in proteomics, diagnosis or drug delivery. Chimerical proteins made of Anx5 fused to an antibody-binding moiety or linked to cell-adhesion peptides allow the construction of 2D platforms for anchoring antibodies, proteins or cells in a controlled orientation and density.5 Gold particles functionalized with oriented Anx5 or Anx5-fusion proteins are used for labelling membrane fragments exposing phosphatidylserine molecules, such as apoptotic membranes or plasmatic microparticles, opening novel strategies for the separation and the analysis of circulating cell membrane fragments.
1F. Oling, W. Bergsma-Schutter and A. Brisson J. Struct. Biol. 2000, 133, 55-63.
2Reviakine, I., Bergsma-Schutter, W. and Brisson, A. J. Struct. Biol. 1998, 121, 356-61.
3Richter, R.P.; Lai-Kee-Him, J.; Tessier, C.; Brisson, A. R. Biophys. J.2005, 89, 3372-3385.
4Richter, R.P.; Bérat, R; Brisson, A. R. Langmuir 2006, 22, 3497-3505.
6Bérat, R.; Rémy-Zolghadry, M.; Gounou, C.; Manigand, C.; Tan, S.; Saltó, C.; Arenas, E.; Bordenave, L; Brisson, A. R. Biointerphases, 2007, 2, 165-172.