Nanowire-Imposed Geometrical Control in Studies of Actomyosin Motor Function
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/7410997
- author
- Lard, Mercy
LU
; ten Siethoff, Lasse
; Generosi, Johanna
LU
; Persson, Malin
; Linke, Heiner
LU
and Mansson, Alf
- organization
- publishing date
- 2015
- 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}}, }