Toward smart surfaces for bionanomotor applications

COLL 456

Jad A. Jaber1, Mark C. Wang1, P. Bryant Chase2, and Joseph B. Schlenoff1. (1) Department of Chemistry and Biochemistry, Center for Materials Research and Technology (MARTECH), The Florida State University, Dittmer Research Building, Tallahassee, FL 32306, (2) Department of Biological Sciences, Program in Moleculer Biophysics, Florida State University, Tallahassee, FL 32306
Nanoscale surface coatings are being developed that support functional, controlled interactions between proteins and synthetic nano-components in miniaturized devices. One example involves naturally occurring motor proteins such as myosin coupled with actin filaments to power micro- and nano-scale motions; an advantage of biomolecular motors is that their peak efficiency can be 30 – 50%. In this work, electrostatic layer-by-layer assembly of oppositely charged polymers is employed for the preparation of uniform thin film coating. A solution of heavy meromyosin (HMM) was applied to immobilize the molecules on a monolayer of the polyelectrolyte PAH, poly(allylamine hydrochloride), and multilayers consisting of 11-41 layers of alternating polypositive PAH/polynegative PSS (polystyrene sulfonate) polyelectrolytes. Myosin driven motion of actin filaments labeled with rhodamine-phalloidin was recorded at 30°C using epifluorescence microscopy. Actin filaments were found to have a mean speed of 2.9 ± 0.1 µm/sec on the multilayer surface compared to 2.5 ± 0.1 µm/sec on the monolayer surface. The ability to control actomyosin interactions can be refined by creating nano-scale structural features or reversibly changing the host environment in response to external stimuli . While micro-contact printing with a water-insoluble charged block copolymer restricted filament motion on patterned PAH tracks, the formation and temperature behavior of ionically modified poly(N-isopropylacrylamide) (NIPAM)-based thermosensitive multilayers, were studied and shown to have a reversible hydrophobic/hydrophilic behavior. Their ability to influence protein interactions will be presented.