Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.3/1963

Title

Manipulation of the motility of protein molecular motors on microfabricated substrates

Author(s)

Dos Remedios, Cristobal G.;  Kekic, Murat;  Mahanivong, Chittladda;  Nicolau, Dan V.;  Pham, Duy K.;  Wright, Jonathon P.

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 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

Source

Biomedical microdevices, Vol. 4, no. 2 (May 2002), pp. 111-116

Publication year

2002

Keyword(s)

in vitro motility assays;  protein attachment;  laser ablation

Publisher

Kluwer Academic Publishers

Format

pp. 111-116

ISSN

1387-2176

Publisher URL

http://dx.doi.org/doi:10.1023/A:1014631130726

Copyright

© 2002 Kluwer Academic Publishers.

Peer reviewed