Nanoscale Topography Mediates the Adhesion of F‑Actin
Using a controllable nanoengineered surface that alters the dynamics of filamentous actin (F-actin) adhesion, we studied the tunability of biomolecular surface attachment. By grafting aminated nanoparticles, NPs, with diameters ranging from 12 to 85 nm to a random copolymer film, precise control ove...
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Veröffentlicht in: | Langmuir 2012-08, Vol.28 (33), p.12216-12224 |
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creator | Caporizzo, Matthew A Sun, Yujie Goldman, Yale E Composto, Russell J |
description | Using a controllable nanoengineered surface that alters the dynamics of filamentous actin (F-actin) adhesion, we studied the tunability of biomolecular surface attachment. By grafting aminated nanoparticles, NPs, with diameters ranging from 12 to 85 nm to a random copolymer film, precise control over surface roughness parameters is realized. The ability to selectively generate monodisperse or polydisperse features of varying size and areal density leads to immobilized, side-on wobbly, or end-on F-actin binding as characterized by total internal reflection fluorescence (TIRF) microscopy. The interaction between the surface and actin is explained by a worm-like chain model that balances the bending energy penalty required for actin to conform to topographical features with the electrostatic attraction engineered into the surface. A Myosin V motility assay demonstrates that electrostatically immobilized actin retains its ability to direct myosin motion, indicating that nanoengineered surfaces are attractive candidates for biomolecular device fabrication. |
doi_str_mv | 10.1021/la302250x |
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By grafting aminated nanoparticles, NPs, with diameters ranging from 12 to 85 nm to a random copolymer film, precise control over surface roughness parameters is realized. The ability to selectively generate monodisperse or polydisperse features of varying size and areal density leads to immobilized, side-on wobbly, or end-on F-actin binding as characterized by total internal reflection fluorescence (TIRF) microscopy. The interaction between the surface and actin is explained by a worm-like chain model that balances the bending energy penalty required for actin to conform to topographical features with the electrostatic attraction engineered into the surface. A Myosin V motility assay demonstrates that electrostatically immobilized actin retains its ability to direct myosin motion, indicating that nanoengineered surfaces are attractive candidates for biomolecular device fabrication.</description><subject>Actin Cytoskeleton - chemistry</subject><subject>Actins - chemistry</subject><subject>Adsorption</subject><subject>Chemistry</subject><subject>Colloidal state and disperse state</subject><subject>Exact sciences and technology</subject><subject>General and physical chemistry</subject><subject>Models, Molecular</subject><subject>Nanotechnology - methods</subject><subject>Physical and chemical studies. Granulometry. 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Electrokinetic phenomena</topic><topic>Protein Conformation</topic><topic>Silicon Dioxide - chemistry</topic><topic>Static Electricity</topic><topic>Surface Properties</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Caporizzo, Matthew A</creatorcontrib><creatorcontrib>Sun, Yujie</creatorcontrib><creatorcontrib>Goldman, Yale E</creatorcontrib><creatorcontrib>Composto, Russell J</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Langmuir</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Caporizzo, Matthew A</au><au>Sun, Yujie</au><au>Goldman, Yale E</au><au>Composto, Russell J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nanoscale Topography Mediates the Adhesion of F‑Actin</atitle><jtitle>Langmuir</jtitle><addtitle>Langmuir</addtitle><date>2012-08-21</date><risdate>2012</risdate><volume>28</volume><issue>33</issue><spage>12216</spage><epage>12224</epage><pages>12216-12224</pages><issn>0743-7463</issn><eissn>1520-5827</eissn><coden>LANGD5</coden><abstract>Using a controllable nanoengineered surface that alters the dynamics of filamentous actin (F-actin) adhesion, we studied the tunability of biomolecular surface attachment. 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subjects | Actin Cytoskeleton - chemistry Actins - chemistry Adsorption Chemistry Colloidal state and disperse state Exact sciences and technology General and physical chemistry Models, Molecular Nanotechnology - methods Physical and chemical studies. Granulometry. Electrokinetic phenomena Protein Conformation Silicon Dioxide - chemistry Static Electricity Surface Properties |
title | Nanoscale Topography Mediates the Adhesion of F‑Actin |
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