Diffusion Dynamics of Motor-Driven Transport: Gradient Production and Self-Organization of Surfaces.
(2008) In Langmuir 24(23). p.13509-13517- Abstract
- The interaction between cytoskeletal filaments (e.g., actin filaments) and molecular motors (e.g., myosin) is the basis for many aspects of cell motility and organization of the cell interior. In the in vitro motility assay (IVMA), cytoskeletal filaments are observed while being propelled by molecular motors adsorbed to artificial surfaces (e.g., in studies of motor function). Here we integrate ideas that cytoskeletal filaments may be used as nanoscale templates in nanopatterning with a novel approach for the production of surface gradients of biomolecules and nanoscale topographical features. The production of such gradients is challenging but of increasing interest (e.g., in cell biology). First, we show that myosin-induced actin... (More)
- The interaction between cytoskeletal filaments (e.g., actin filaments) and molecular motors (e.g., myosin) is the basis for many aspects of cell motility and organization of the cell interior. In the in vitro motility assay (IVMA), cytoskeletal filaments are observed while being propelled by molecular motors adsorbed to artificial surfaces (e.g., in studies of motor function). Here we integrate ideas that cytoskeletal filaments may be used as nanoscale templates in nanopatterning with a novel approach for the production of surface gradients of biomolecules and nanoscale topographical features. The production of such gradients is challenging but of increasing interest (e.g., in cell biology). First, we show that myosin-induced actin filament sliding in the IVMA can be approximately described as persistent random motion with a diffusion coefficient ( D) given by a relationship analogous to the Einstein equation ( D = kT/gamma). In this relationship, the thermal energy ( kT) and the drag coefficient (gamma) are substituted by a parameter related to the free-energy transduction by actomyosin and the actomyosin dissociation rate constant, respectively. We then demonstrate how the persistent random motion of actin filaments can be exploited in conceptually novel methods for the production of actin filament density gradients of predictable shapes. Because of regularly spaced binding sites (e.g., lysines and cysteines) the actin filaments act as suitable nanoscale scaffolds for other biomolecules (tested for fibronectin) or nanoparticles. This forms the basis for secondary chemical and topographical gradients with implications for cell biological studies and biosensing. (Less)
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https://lup.lub.lu.se/record/1271753
- author
- organization
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Langmuir
- volume
- 24
- issue
- 23
- pages
- 13509 - 13517
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000261216500043
- pmid:18989944
- scopus:62649141432
- pmid:18989944
- ISSN
- 0743-7463
- DOI
- 10.1021/la8016112
- language
- English
- LU publication?
- yes
- id
- 7d8cecb3-e3aa-42f5-bf3b-a4215f44a186 (old id 1271753)
- date added to LUP
- 2016-04-01 12:08:55
- date last changed
- 2022-01-26 23:30:46
@article{7d8cecb3-e3aa-42f5-bf3b-a4215f44a186,
abstract = {{The interaction between cytoskeletal filaments (e.g., actin filaments) and molecular motors (e.g., myosin) is the basis for many aspects of cell motility and organization of the cell interior. In the in vitro motility assay (IVMA), cytoskeletal filaments are observed while being propelled by molecular motors adsorbed to artificial surfaces (e.g., in studies of motor function). Here we integrate ideas that cytoskeletal filaments may be used as nanoscale templates in nanopatterning with a novel approach for the production of surface gradients of biomolecules and nanoscale topographical features. The production of such gradients is challenging but of increasing interest (e.g., in cell biology). First, we show that myosin-induced actin filament sliding in the IVMA can be approximately described as persistent random motion with a diffusion coefficient ( D) given by a relationship analogous to the Einstein equation ( D = kT/gamma). In this relationship, the thermal energy ( kT) and the drag coefficient (gamma) are substituted by a parameter related to the free-energy transduction by actomyosin and the actomyosin dissociation rate constant, respectively. We then demonstrate how the persistent random motion of actin filaments can be exploited in conceptually novel methods for the production of actin filament density gradients of predictable shapes. Because of regularly spaced binding sites (e.g., lysines and cysteines) the actin filaments act as suitable nanoscale scaffolds for other biomolecules (tested for fibronectin) or nanoparticles. This forms the basis for secondary chemical and topographical gradients with implications for cell biological studies and biosensing.}},
author = {{Vikhorev, Petr and Vikhoreva, Natalia and Sundberg, Mark and Balaz, Martina and Albet-Torres, Nuria and Bunk, Richard and Kvennefors, Anders and Liljesson, Kenneth and Nicholls, Ian and Nilsson, Leif and Omling, Pär and Tågerud, Sven and Montelius, Lars and Månsson, Alf}},
issn = {{0743-7463}},
language = {{eng}},
number = {{23}},
pages = {{13509--13517}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Langmuir}},
title = {{Diffusion Dynamics of Motor-Driven Transport: Gradient Production and Self-Organization of Surfaces.}},
url = {{http://dx.doi.org/10.1021/la8016112}},
doi = {{10.1021/la8016112}},
volume = {{24}},
year = {{2008}},
}