Synthetic proteo-nucleic structures (PDNA) encompassing a ss-DNA sequence covalently attached to a cytochrome b5-derived protein domain through a synthetic linker were designed. PDNAs can bind to natural or supported membranes through an histidine-tag-nickel-NTA modified phospholipids. Alternatively the structures can be attached, while keeping free lateral diffusion capabilities, by interaction of the protein his-tag with a substrate supported field of nickel ions. Floating individual tiles can be in turn self-assembled together in the presence of half-complementary ss-DNA, to form surface constrained chains of protein domains linked by ds-stranded DNA segments.
A combination of experimental (single molecule confocal microscopy, surface plasmon resonance imagery, static atomic force microscopy) and numeric simulation approaches were used to characterize factors controlling self-assembly on the surface. Dynamic of interaction between PDNA assemblies was investigated using high speed AFM in solution and evidenced unusual modes of lateral diffusion of the structures on mica surface and transient formation of linear and cycling complexes involving base pairing between very short DNA stretches.
Dynamic AFM thus constitutes a very promising tool for the characterization of the time resolved aspects of the self-assembly of biomimetic structures.
This poster was presented at NanoBioViews 2009; 14-15 October 2009: http://www.nanobioviews.net
Click this link to view the complete poster as a PDF
Contact:
Aude Laisné
Centre de Génétique Moléculaire and Institut des Sciences du Végétal of CNRS
Avenue de la Terrasse
91190 Gif-sur-Yvette, France
aude.laisne@cgm.cnrs-gif.fr
Authors:
Aude Laisné
Eric Lesniewska
Denis Pompon
Keywords: AFM Atomic force microscopy confocal microscopy high speed AFM PDNA SPM surface plasmon resonance imagery
Reader comments (0)