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Proceedings Paper

Biological transport in a microfabricated device: active immunochromatography with motorized antibodies
Author(s): Loren Limberis; Russell J. Stewart
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Paper Abstract

Kinesin motor proteins transduce chemical energy released by adenosine triphosphate hydrolysis into mechanical force and motion along microtubule tracks. Biological cells use kinesin motors to transport intracellular components to specific cellular locations. Our goal is to mimic some aspects of kinesin's cellular function and apply them to an active separation microdevice. Here we report the coupling of cargo-binding domains to recombinant kinesin. Metal- chelating Pluronic surfactants were used to specifically co- immobilize recombinant kinesin motor proteins and two immunoglobulin-(IgG) binding domains of protein A on the surface of polystyrene beads. Monoclonal antibodies, the cargo-binding domains, were indirectly coupled to kinesin on the beads through the IgG-binding domains. These motorized antibodies are capable of specifically binding virtually any cargo (antigens) and transporting them along microtubule tracks to different locations or compartments in an active separation microdevice.

Paper Details

Date Published: 10 September 1998
PDF: 10 pages
Proc. SPIE 3515, Microfluidic Devices and Systems, (10 September 1998); doi: 10.1117/12.322097
Show Author Affiliations
Loren Limberis, Univ. of Utah (United States)
Russell J. Stewart, Univ. of Utah (United States)


Published in SPIE Proceedings Vol. 3515:
Microfluidic Devices and Systems
A. Bruno Frazier; Chong Hyuk Ahn, Editor(s)

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