19 November 2001 Controlling actin motility on microfabricated linear channels
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Abstract
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 labelled 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 labelled 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.
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Chitladda Mahanivong, Chitladda Mahanivong, Jonathan P. Wright, Jonathan P. Wright, Murat Kekic, Murat Kekic, Duy K. Pham, Duy K. Pham, Cristobal dos Remedios, Cristobal dos Remedios, Dan V. Nicolau, Dan V. Nicolau, } "Controlling actin motility on microfabricated linear channels", Proc. SPIE 4590, BioMEMS and Smart Nanostructures, (19 November 2001); doi: 10.1117/12.454621; https://doi.org/10.1117/12.454621
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