Antibodies Covalently Immobilized on Actin Filaments for Fast Myosin Driven Analyte Transport
Kumar, Saroj ; ten Siethoff, Lasse ; Persson, Malin ; Lard, Mercy LU ; Kronnie, Geertruy Te ; Linke, Heiner LU
and Mansson, Alf
(2012)
In PLoS ONE
7(10).
- Abstract
- Biosensors would benefit from further miniaturization, increased detection rate and independence from external pumps and other bulky equipment. Whereas transportation systems built around molecular motors and cytoskeletal filaments hold significant promise in the latter regard, recent proof-of-principle devices based on the microtubule-kinesin motor system have not matched the speed of existing methods. An attractive solution to overcome this limitation would be the use of myosin driven propulsion of actin filaments which offers motility one order of magnitude faster than the kinesin-microtubule system. Here, we realized a necessary requirement for the use of the actomyosin system in biosensing devices, namely covalent attachment of... (More)
- Biosensors would benefit from further miniaturization, increased detection rate and independence from external pumps and other bulky equipment. Whereas transportation systems built around molecular motors and cytoskeletal filaments hold significant promise in the latter regard, recent proof-of-principle devices based on the microtubule-kinesin motor system have not matched the speed of existing methods. An attractive solution to overcome this limitation would be the use of myosin driven propulsion of actin filaments which offers motility one order of magnitude faster than the kinesin-microtubule system. Here, we realized a necessary requirement for the use of the actomyosin system in biosensing devices, namely covalent attachment of antibodies to actin filaments using heterobifunctional cross-linkers. We also demonstrated consistent and rapid myosin II driven transport where velocity and the fraction of motile actin filaments was negligibly affected by the presence of antibody-antigen complexes at rather high density (>20 mu m(-1)). The results, however, also demonstrated that it was challenging to consistently achieve high density of functional antibodies along the actin filament, and optimization of the covalent coupling procedure to increase labeling density should be a major focus for future work. Despite the remaining challenges, the reported advances are important steps towards considerably faster nanoseparation than shown for previous molecular motor based devices, and enhanced miniaturization because of high bending flexibility of actin filaments. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3174923
- author
- Kumar, Saroj
; ten Siethoff, Lasse
; Persson, Malin
; Lard, Mercy
LU
; Kronnie, Geertruy Te
; Linke, Heiner
LU
and Mansson, Alf
- organization
- publishing date
- 2012
- type
- Contribution to journal
- publication status
- published
- subject
- in
- PLoS ONE
- volume
- 7
- issue
- 10
- publisher
- Public Library of Science (PLoS)
- external identifiers
-
- wos:000309454000032
- scopus:84867081685
- pmid:23056279
- ISSN
- 1932-6203
- DOI
- 10.1371/journal.pone.0046298
- language
- English
- LU publication?
- yes
- id
- ab85a339-2a08-42f9-bd9a-103fbfdc225f (old id 3174923)
- date added to LUP
- 2016-04-01 14:31:45
- date last changed
- 2023-11-13 08:31:39
@article{ab85a339-2a08-42f9-bd9a-103fbfdc225f,
abstract = {{Biosensors would benefit from further miniaturization, increased detection rate and independence from external pumps and other bulky equipment. Whereas transportation systems built around molecular motors and cytoskeletal filaments hold significant promise in the latter regard, recent proof-of-principle devices based on the microtubule-kinesin motor system have not matched the speed of existing methods. An attractive solution to overcome this limitation would be the use of myosin driven propulsion of actin filaments which offers motility one order of magnitude faster than the kinesin-microtubule system. Here, we realized a necessary requirement for the use of the actomyosin system in biosensing devices, namely covalent attachment of antibodies to actin filaments using heterobifunctional cross-linkers. We also demonstrated consistent and rapid myosin II driven transport where velocity and the fraction of motile actin filaments was negligibly affected by the presence of antibody-antigen complexes at rather high density (>20 mu m(-1)). The results, however, also demonstrated that it was challenging to consistently achieve high density of functional antibodies along the actin filament, and optimization of the covalent coupling procedure to increase labeling density should be a major focus for future work. Despite the remaining challenges, the reported advances are important steps towards considerably faster nanoseparation than shown for previous molecular motor based devices, and enhanced miniaturization because of high bending flexibility of actin filaments.}},
author = {{Kumar, Saroj and ten Siethoff, Lasse and Persson, Malin and Lard, Mercy and Kronnie, Geertruy Te and Linke, Heiner and Mansson, Alf}},
issn = {{1932-6203}},
language = {{eng}},
number = {{10}},
publisher = {{Public Library of Science (PLoS)}},
series = {{PLoS ONE}},
title = {{Antibodies Covalently Immobilized on Actin Filaments for Fast Myosin Driven Analyte Transport}},
url = {{https://lup.lub.lu.se/search/files/4026206/3217286.pdf}},
doi = {{10.1371/journal.pone.0046298}},
volume = {{7}},
year = {{2012}},
}