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Proceedings Paper

Controlling actin motility on microfabricated linear channels
Author(s): Chitladda Mahanivong; Jonathan P. Wright; Murat Kekic; Duy K. Pham; Cristobal dos Remedios; Dan V. Nicolau
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Paper 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.

Paper Details

Date Published: 19 November 2001
PDF: 7 pages
Proc. SPIE 4590, BioMEMS and Smart Nanostructures, (19 November 2001); doi: 10.1117/12.454621
Show Author Affiliations
Chitladda Mahanivong, Swinburne Univ. of Technology (Australia)
Jonathan P. Wright, Swinburne Univ. of Technology (Australia)
Murat Kekic, Univ. of Sydney (Australia)
Duy K. Pham, Swinburne Univ. of Technology (Australia)
Cristobal dos Remedios, Univ. of Sydney (Australia)
Dan V. Nicolau, Swinburne Univ. of Technology (Australia)

Published in SPIE Proceedings Vol. 4590:
BioMEMS and Smart Nanostructures
Laszlo B. Kish; Erol C. Harvey; William B. Spillman Jr., Editor(s)

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