title: Nanoscale topography mediates the adhesion of F-actin.
abstract: Using a controllable nanoengineered surface that alters the dynamics of filamentous actin (F-actin) adhesion, we studied the tunability of biomolecular surface attachment. By grafting aminated nanoparticles, NPs, with diameters ranging from 12 to 85 nm to a random copolymer film, precise control over surface roughness parameters is realized. The ability to selectively generate monodisperse or polydisperse features of varying size and areal density leads to immobilized, side-on wobbly, or end-on F-actin binding as characterized by total internal reflection fluorescence (TIRF) microscopy. The interaction between the surface and actin is explained by a worm-like chain model that balances the bending energy penalty required for actin to conform to topographical features with the electrostatic attraction engineered into the surface. A Myosin V motility assay demonstrates that electrostatically immobilized actin retains its ability to direct myosin motion, indicating that nanoengineered surfaces are attractive candidates for biomolecular device fabrication.
authors: Department of Materials Science and Engineering, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
authors: Matthew A
authors: MA
authors: Caporizzo
authors: Yujie
authors: Y
authors: Sun
authors: Yale E
authors: YE
authors: Goldman
authors: Russell J
authors: RJ
authors: Composto
mesh_terms: D008841:Actin Cytoskeleton / Q000737:chemistry; D000199:Actins / Q000737:chemistry*; D000327:Adsorption; D008958:Models, Molecular; D036103:Nanotechnology / Q000379:methods*; D011487:Protein Conformation; D012822:Silicon Dioxide / Q000737:chemistry; D055672:Static Electricity; D013499:Surface Properties
chemical_list: D000199:Actins; D012822:Silicon Dioxide