Selective assembly and alignment of actin filaments with desired polarity on solid substrates
We report a new strategy to selectively assemble and align filamentous actin (F-actin) onto desired locations on a solid substrate with a specific structural polarity. In this strategy, biotinylated gelsolin caps the structural minus end of F-actin so that the F-actin binds onto a streptavidin patte...
Publié dans: | Langmuir : the ACS journal of surfaces and colloids. - 1985. - 22(2006), 21 vom: 10. Okt., Seite 8635-8 |
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Auteur principal: | |
Autres auteurs: | , , , |
Format: | Article |
Langue: | English |
Publié: |
2006
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Accès à la collection: | Langmuir : the ACS journal of surfaces and colloids |
Sujets: | Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Actins Biotin 6SO6U10H04 |
Résumé: | We report a new strategy to selectively assemble and align filamentous actin (F-actin) onto desired locations on a solid substrate with a specific structural polarity. In this strategy, biotinylated gelsolin caps the structural minus end of F-actin so that the F-actin binds onto a streptavidin pattern with a specific structural polarity. We also demonstrate that an electric field can be utilized to align bound F-actin along a desired direction. This can be one of the major technical breakthroughs toward the assembly of nanomechanical systems based on myosin biomotors |
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Description: | Date Completed 06.09.2007 Date Revised 21.11.2013 published: Print Citation Status MEDLINE |
ISSN: | 1520-5827 |