Search Swinburne Research Bank
Home List of Titles Adsorption-induced inactivation of heavy meromyosin on polymer surfaces imposes effective drag force on sliding actin filaments in vitro
Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.3/5947
- Adsorption-induced inactivation of heavy meromyosin on polymer surfaces imposes effective drag force on sliding actin filaments in vitro
- Hanson, Kristi L.; Solana, Gerardin; Vaidyanathan, Viswanathan; Nicolau, Dan V.
- Actin and myosin are of interest as potential force-generating elements in engineered nanodevices. Such applications require surface coatings which are both biocompatible and amenable to nanolithographic processing, but the manner in which surfaces modulate motor protein function has not been rigorously studied. Here we examine motor protein surface density and bioactivity on a variety of polymer surfaces, and compare the results to in vitro actomyosin motility characteristics. Filament velocities were found to be controlled by the proportion, rather than density, of active heavy meromyosin (HMM), consistent with the imposition of an effective drag force by inactivated HMM due to weak actin-binding interactions. Interpretation of the results with respect to previous models suggests that the inactive HMM fraction has no force-generating ability, and that the effective drag imposed on polystyrene is lower than that on methacrylate polymers and nitrocellulose, consistent with a higher degree of protein denaturation on aromatic surface structures.
- Publication type
- Conference paper
- Research centre
- Swinburne University of Technology. Faculty of Engineering and Industrial Sciences. Industrial Research Institute Swinburne
- Proceedings 2006 International Conference on Microtechnologies in Medicine and Biology, Okinawa, Japan, 09-12 May 2006, p. 151-154
- Publication year
- Actin-binding interaction; Active heavy meromyosin; Actomyosin mechanics; Actomyosin motility characteristics; Adsorption; Adsorption-induced inactivation; Aromatic surface structure; Bioactivity; Drag force; Engineered nanodevices; Force-generating elements; In vitro motility assay; Microbalances; Molecular biophysics; Motor protein function; Nanolithographic processing; Nanolithography; Nitrocellulose; Polymer films; Polymer surface coating; Protein adsorption; Protein denaturation; Proteins; Quartz crystal microbalance; Sliding actin filaments; Surface density
- Publisher URL
- Copyright © 2006 IEEE.
- Peer reviewed