Laboratory of Molecular Imaging and Nano-Bio-Technology

Head : Alain D.R. Brisson, Prof. Université Bordeaux 1
Research Team - Equipment - Highlights - Publications

Research in the Laboratory of Molecular Imaging and Nano-Bio-Technology (LMINT) has two main orientations:

1) Structure-Function studies of protein-membrane complexes.

Our objectives are:

1. to reveal the high-resolution structure of supramolecular complexes formed at the level of biological membranes ­either by soluble or transmembrane proteins- in physiological and pathological conditions;
2. to elucidate the mechanism of assembly and the function of such complexes.

2) Nano-Bio-Technology.

Our objective is to develop technologies based on 2D arrays of functionalized proteins deposited on solid supports for the construction of composite assemblies.

Ongoing projects:

• Role of annexins in organizing raft domains;
• Interaction of the ß-amyloid peptide with model membranes;
• AFM imaging of immobilized nicotinic acetylcholine receptor protein;
• Formation of Solid-supported Lipid Bilayers on various surfaces and growth of protein 2D crystals.

Experimentally, the LMINT specializes in advanced methods of molecular imaging at sub-nm resolution - including cryo-electron microscopy, image analysis and Atomic Force Microscopy - and in surface-sensitive methods - particularly the Quartz Crystal Microbalance with Dissipation monitoring (QCM-D).

The LMINT was created on September 1, 2001

• Brisson, Alain : Head
• Lambert, Olivier : CNRS Researcher
• Lai Kee Him, Joséphine : Post-doctoral researcher
• Chami, Mohamed : Post-doctoral researcher
• Richter, Ralf : PhD student
• Buzhynskyy, Nick : PhD student
• Tessier, Béatrice : Technical Assisitant

Vacancy for assistant professor position in 2002.

• Cryo-electron Microscope FEI Tecnai F-20 (200 kV)
• Cryo-electron Microscope FEI EM120 (120 kV)
• 2 Cameras SSCCD 2kx2k Gatan (in 2002)
• 2 Cryo-holders Gatan
• Cryo-station Leica
• Carbon evaporator Edwards
• Atomic Force Microscope Nanoscope IV
• Quartz Crystal Microbalance with Dissipation Monitoring (QCM-D, Q-Sense, Gothenburg)
• FPLC-HPLC Akta-Purifier Amersham-Pharmacia
• Ultracentrifuge Opti Max-E Beckman

Determination of the 3D structure of uroplakine, the major membrane protein from mammalian urinary bladder, by Cryo-Electron Crystallography, at ~ 1 nm resolution (work performed in A. Brisson's former group at the University of Groningen) (J. Mol. Biol. 2001, 314, 233-240)	Real-time AFM imaging of the transition between two 2D crystalline phases formed by Annexin A5 on solid-suported phospholipid bilayers (Langmuir 2001, 17, 1680-1686).
Process of formation of SPB (solid-supported phospholipid bialyers) on mica revealed in real time by AFM. (Langmuir 2000, 16, 1806-1815).	Comparison of the membrane-bound and soluble forms of Annexin A5, at 6 Å resolution, by hybrid - cryo-EM and X-ray - crystallography (J. Mol. Biol. 2000, 304, 561-573).
Transfer of DNA into proteoliposomes and DNA condensation revealed by Cryo-EM (work performed by O. Lambert in J.L. Rigaud's group) (P.N.A.S. 2000, 97, 7248-7253).

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