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Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.3/1963
- Manipulation of the motility of protein molecular motors on microfabricated substrates
- Dos Remedios, Cristobal G.; Kekic, Murat; Mahanivong, Chittladda; Nicolau, Dan V.; Pham, Duy K.; Wright, Jonathon P.
- Heavy meromyosin (HMM), a proteolytically cleaved derivative of myosin has previously been shown to interact with actin in well-established in vitro motility assays on nitrocellulose surfaces. In this study, the assays were conducted to demonstrate that the motility of actin filaments is confined in the micron-sized channels fabricated via laser ablation in a layer of the photosensitive resist polymer O-acryloyloxime acetophenone oxime (AAPO). A solution containing myosin labeled with fluorophore 5-iodoacetamidofluorescein (5-IAF) was applied to the microfabricated AAPO surface and shown to bind specifically to the micron-size channels. In the motility assay, HMM, rhodamine-phalloidin labeled actin and ATP were sequentially added and the movement of the actin filaments was observed by fluorescence microscopy and recorded with a CCD camera. The experiments prove that although the actin filaments show an only-partial propensity for attachment in myosin-rich areas, their motility is confined to a large extent in micro-channels.
- Publication type
- Journal article
- Research centre
- Swinburne University of Technology. Industrial Research Institute Swinburne
- Biomedical microdevices , Vol. 4, no. 2 (May 2002), pp. 111-116
- Publication year
- Kluwer Academic Publishers
- pp. 111-116
- Publisher URL
- © 2002 Kluwer Academic Publishers.