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Nanowire-Imposed Geometrical Control in Studies of Actomyosin Motor Function

Lard, Mercy LU ; ten Siethoff, Lasse ; Generosi, Johanna LU ; Persson, Malin ; Linke, Heiner LU orcid and Mansson, Alf (2015) In IEEE Transactions on Nanobioscience 14(3). p.289-297
Abstract
Recently, molecular motor gliding assays with actin and myosin from muscle have been realized on semiconductor nanowires coated with Al2O3. This opens for unique nanotechnological applications and novel fundamental studies of actomyosin motor function. Here, we provide a comparison of myosin-driven actin filament motility on Al2O3 to both nitrocellulose and trimethylchlorosilane derivatized surfaces. We also show that actomyosin motility on the less than 200 nm wide tips of arrays of Al2O3-coated nanowires can be used to control the number, and density, of myosin-actin attachment points. Results obtained using nanowire arrays with different inter-wire spacing are consistent with the idea that the actin filament sliding velocity is... (More)
Recently, molecular motor gliding assays with actin and myosin from muscle have been realized on semiconductor nanowires coated with Al2O3. This opens for unique nanotechnological applications and novel fundamental studies of actomyosin motor function. Here, we provide a comparison of myosin-driven actin filament motility on Al2O3 to both nitrocellulose and trimethylchlorosilane derivatized surfaces. We also show that actomyosin motility on the less than 200 nm wide tips of arrays of Al2O3-coated nanowires can be used to control the number, and density, of myosin-actin attachment points. Results obtained using nanowire arrays with different inter-wire spacing are consistent with the idea that the actin filament sliding velocity is determined both by the total number and the average density of attached myosin heads along the actin filament. Further, the results are consistent with buckling of long myosin-free segments of the filaments as a factor underlying reduced velocity. On the other hand, the findings do not support a mechanistic role in decreasing velocity, of increased nearest neighbor distance between available myosin heads. Our results open up for more advanced studies that may use nanowire-based structures for fundamental investigations of molecular motors, including the possibility to create a nanowire-templated bottom-up assembly of 3D, muscle-like structures. (Less)
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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Actin, aluminum oxide, in vitro motility assay, myosin, oxide-coated, nanowire, sarcomere
in
IEEE Transactions on Nanobioscience
volume
14
issue
3
pages
289 - 297
publisher
IEEE - Institute of Electrical and Electronics Engineers Inc.
external identifiers
  • wos:000355321100005
  • scopus:84930670434
  • pmid:25823040
ISSN
1558-2639
DOI
10.1109/TNB.2015.2412036
language
English
LU publication?
yes
id
4c38d0f4-a6ae-4355-980a-034668165f87 (old id 7410997)
date added to LUP
2016-04-01 10:06:25
date last changed
2023-10-11 18:27:47
@article{4c38d0f4-a6ae-4355-980a-034668165f87,
  abstract     = {{Recently, molecular motor gliding assays with actin and myosin from muscle have been realized on semiconductor nanowires coated with Al2O3. This opens for unique nanotechnological applications and novel fundamental studies of actomyosin motor function. Here, we provide a comparison of myosin-driven actin filament motility on Al2O3 to both nitrocellulose and trimethylchlorosilane derivatized surfaces. We also show that actomyosin motility on the less than 200 nm wide tips of arrays of Al2O3-coated nanowires can be used to control the number, and density, of myosin-actin attachment points. Results obtained using nanowire arrays with different inter-wire spacing are consistent with the idea that the actin filament sliding velocity is determined both by the total number and the average density of attached myosin heads along the actin filament. Further, the results are consistent with buckling of long myosin-free segments of the filaments as a factor underlying reduced velocity. On the other hand, the findings do not support a mechanistic role in decreasing velocity, of increased nearest neighbor distance between available myosin heads. Our results open up for more advanced studies that may use nanowire-based structures for fundamental investigations of molecular motors, including the possibility to create a nanowire-templated bottom-up assembly of 3D, muscle-like structures.}},
  author       = {{Lard, Mercy and ten Siethoff, Lasse and Generosi, Johanna and Persson, Malin and Linke, Heiner and Mansson, Alf}},
  issn         = {{1558-2639}},
  keywords     = {{Actin; aluminum oxide; in vitro motility assay; myosin; oxide-coated; nanowire; sarcomere}},
  language     = {{eng}},
  number       = {{3}},
  pages        = {{289--297}},
  publisher    = {{IEEE - Institute of Electrical and Electronics Engineers Inc.}},
  series       = {{IEEE Transactions on Nanobioscience}},
  title        = {{Nanowire-Imposed Geometrical Control in Studies of Actomyosin Motor Function}},
  url          = {{http://dx.doi.org/10.1109/TNB.2015.2412036}},
  doi          = {{10.1109/TNB.2015.2412036}},
  volume       = {{14}},
  year         = {{2015}},
}