AVS 46th International Symposium
    Biomaterial Interfaces Group Monday Sessions
       Session BI-MoA

Paper BI-MoA1
Formation of 2D Crystals of Proteins on Solid-Supported Lipid Bilayers Followed by AFM

Monday, October 25, 1999, 2:00 pm, Room 613/614

Session: Protein Solid-Surface Interactions I
Presenter: A. Brisson, University of Groningen, The Netherlands
Authors: A. Brisson, University of Groningen, The Netherlands
I. Reviakine, University of Groningen, The Netherlands
W. Bergsma-Schutter, University of Groningen, The Netherlands
N. Govorukhina, University of Groningen, The Netherlands
S. Mazeres, University of Groningen, The Netherlands
Correspondent: Click to Email
The possibility of assembling macromolecules or particles in a controlled manner on solid surfaces constitutes a central issue in the emerging field of nanotechnology. Methods for ordering proteins as 2D crystals or helical arrays at the level of lipid surfaces have received particular attention in molecular structure determination by electron crystallography. One of these methods, called the lipid layer crystallization method, uses the specific interaction between a protein and a ligand coupled to a l ipid molecule incorporated in a lipid monolayer at the air-water interface.@footnote 1@,@footnote2@,@footnote 3@ Our objective has been twofold: 1) to extend this strategy to the case of solid-liquid interfaces; 2) to develop an in situ method for following the formation of prot ein 2D crystals. Using Atomic Force Microscopy, both processes of formation of lipid bilayers on solid supports (SPB), and of protein 2D crystallization on SPB could be revealed in real time, in a natural aqueous environment, at sub-molecular resolution.@footnote 4@,@footnote 5@ Results will be presented on the crystallization of annexin V, an inhibitor of blood coagulation which binds specifically to negatively charged lipids, and will be compared to Electron Microscopy data of 2D crystals formed on lipid monolayers. This novel experimental approach offers exciting opportunities in basic science for investigating crystallization processes and provides an adequate technology for fabricating protein-containing biofunctional surfaces. @FootnoteText@ @footnote 1@Uzgiris, E.E. & Kornberg, R.D., Nature 301 (1983) 125. @footnote 2@Brisson A. et al., J. Crystal Growth 196 (1999) 456. @footnote 3@Brisson, A. et al., in Crystallization of Proteins and Nucleic Acids, A Practical Approach, Oxford Univ. Pres (in press). @footnote 4@Reviakine, I., Bergsma-Schutter, W. & Brisson, A., J. Struct. Biol. 121 (1998) 356. @footnote 5@Reviakine, I. & Brisson, A., (submitted). .