Homophilic interactions between cadherin fragments at the single molecule level: an AFM study.
We report measurements of the adhesion forces between single E-cadherin fragments anchored on solid surfaces. These fragments consist of the two outermost extracellular domains of the protein. The specificity of the measured rupture forces was demonstrated by Ca2+ exchange experiments. Two series of experiments were performed using two linkers of different rigidity and length. We find that the pull-off force is distributed with a maximum value independent of the linker and logarithmically dependent on the velocity of separation of the two surfaces. Our dynamical results are compatible with previous flow chamber experiments performed with the same fragments and can be compared from a different perspective with previously reported AFM experiments on the full-length extracellular domain of the VE-cadherin. Interestingly, using a rigid linker, we have been able for the first time to evidence the deformation of the cadherin molecule under mechanical stress, a piece of information not accessible with more classical grafting strategies.
du Roure
O
O
Institut Curie, Centre de Recherche, UMR IC/CNRS 168, 26 rue d'Ulm, 75248 Paris Cedex 05 France.
Buguin
A
A
Feracci
H
H
Silberzan
P
P
D015820:Cadherins / Q000737:chemistry*; D002118:Calcium / Q000737:chemistry; D018625:Microscopy, Atomic Force; D008954:Models, Biological; D010446:Peptide Fragments / Q000737:chemistry; D011485:Protein Binding; D013499:Surface Properties
D015820:Cadherins; D010446:Peptide Fragments; D002118:Calcium