Selective attachment of F-actin with controlled length for developing an intelligent nanodevice

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Authors
Wei, Ming-Yuan
Leon, Lenin J.
Lee, Yongkuk
Parks, Denzel
Carroll, Lloyd
Famouri, Parviz
Advisors
Issue Date
2011-04-01
Type
Article
Keywords
Bio-molecular motors , Atomic force microscopy , Surface modification , Photobiotin , Fluorescence microscopy
Research Projects
Organizational Units
Journal Issue
Citation
Wei, M. Y., Leon, L. J., Lee, Y., Parks, D., Carroll, L., & Famouri, P. (2011). Selective attachment of F-actin with controlled length for developing an intelligent nanodevice. Journal of Colloid and Interface Science. 356(1), 182–189. https://doi.org/10.1016/j.jcis.2010.12.079.
Abstract

Development of the nanodevice that myosin-coated beads “walk” on actin filaments (F-actin) tracks for in vitro nanotransportation was hindered due to the difficulty of assembling large-area well-orientated F-actin tracks on the surface. In this work, we present a selective attachment of F-actin with controlled length on a patterned surface by employing biotinylated capped protein gelsolin as intermediate anchoring bridge. A patterned streptavidin layer was formed via coupling with a biotin layer that photo-actively attached to an amine-functionalized glass surface. The patterned film was found stable and homogenous compared to that obtained by microcontact printing method, according to the profiling with fluorescence microscopy. By a secondary blocking process, non-specific binding of F-actin to the patterned surface through electrostatic adsorption can be resisted. The length variation of F-actin as a function of gelsolin concentration was also investigated, implying that F-actin is appropriately of 2.5 μm in average length once F-actin/gelsolin molar ratio is 4:1. Finally, the selective attachment of F-actin was well characterized with quantifying the number of attached F-actin per unit area in the patterned areas over that in blocked areas. The density of F-actin was estimated at c.a. 2 μm2 per actin filament molecule so that the distance between one another actin filament is estimated as c.a. 1.41–1.97 μm. The unique properties of F-actin, e.g. well flexibility or electrical conductivity, make it feasible to lay them down and form unidirectional aligned tracks by fluidic flow or electrical field. This may open a possibility for the long-distant movement of myosin-coated beads, offering a novel discipline for the development of micro-biochip in vitro.


Graphical abstract A selective attachment of F-actin with controlled length on a patterned surface by employing biotinylated capped protein gelsolin as intermediate anchoring bridge was reported, which may open an avenue for the long-distant movement of myosin-coated beads in future work.

Table of Contents
Description
Article published: 2011-01-03. Issue published: 2011-04-01.
Research highlights ► A selective attachment of F-actin with controlled length on a patterned surface. ► Biotinylated capped protein gelsolin as intermediate anchoring bridge. ► Non-specific binding of F-actin via electrostatic adsorption can be resisted. ► Open a possibility for the long-distant movement of myosin-coated beads.
Publisher
Elsevier
Journal
Journal of Colloid and Interface Science
Book Title
Series
PubMed ID
ISSN
0021-9797
1095-7103
EISSN