Electro-detachment of kinesin motor domain from microtubule in silico
Kinesin is a motor protein essential in cellular functions, such as intracellular transport and cell-division, as well as for enabling nanoscopic transport in bio-nanotechnology. Therefore, for effective control of function for nanotechnological applications, it is important to be able to modify the...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Elsevier
2023-01-01
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| Series: | Computational and Structural Biotechnology Journal |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2001037023000193 |
| _version_ | 1797384172693618688 |
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| author | Jiří Průša Michal Cifra |
| author_facet | Jiří Průša Michal Cifra |
| author_sort | Jiří Průša |
| collection | DOAJ |
| description | Kinesin is a motor protein essential in cellular functions, such as intracellular transport and cell-division, as well as for enabling nanoscopic transport in bio-nanotechnology. Therefore, for effective control of function for nanotechnological applications, it is important to be able to modify the function of kinesin. To circumvent the limitations of chemical modifications, here we identify another potential approach for kinesin control: the use of electric forces. Using full-atom molecular dynamics simulations (247,358 atoms, total time ∼ 4.4 μs), we demonstrate, for the first time, that the kinesin-1 motor domain can be detached from a microtubule by an intense electric field within the nanosecond timescale. We show that this effect is field-direction dependent and field-strength dependent. A detailed analysis of the electric forces and the work carried out by electric field acting on the microtubule–kinesin system shows that it is the combined action of the electric field pulling on the β-tubulin C-terminus and the electric-field-induced torque on the kinesin dipole moment that causes kinesin detachment from the microtubule. It is shown, for the first time in a mechanistic manner, that an electric field can dramatically affect molecular interactions in a heterologous functional protein assembly. Our results contribute to understanding of electromagnetic field–biomatter interactions on a molecular level, with potential biomedical and bio-nanotechnological applications for harnessing control of protein nanomotors. |
| first_indexed | 2024-03-08T21:31:39Z |
| format | Article |
| id | doaj.art-d3aeebc94dea4ce8918136d36fbf2863 |
| institution | Directory Open Access Journal |
| issn | 2001-0370 |
| language | English |
| last_indexed | 2024-03-08T21:31:39Z |
| publishDate | 2023-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Computational and Structural Biotechnology Journal |
| spelling | doaj.art-d3aeebc94dea4ce8918136d36fbf28632023-12-21T07:30:47ZengElsevierComputational and Structural Biotechnology Journal2001-03702023-01-012113491361Electro-detachment of kinesin motor domain from microtubule in silicoJiří Průša0Michal Cifra1Institute of Photonics and Electronics of the Czech Academy of Sciences, Prague 18200, CzechiaCorresponding author.; Institute of Photonics and Electronics of the Czech Academy of Sciences, Prague 18200, CzechiaKinesin is a motor protein essential in cellular functions, such as intracellular transport and cell-division, as well as for enabling nanoscopic transport in bio-nanotechnology. Therefore, for effective control of function for nanotechnological applications, it is important to be able to modify the function of kinesin. To circumvent the limitations of chemical modifications, here we identify another potential approach for kinesin control: the use of electric forces. Using full-atom molecular dynamics simulations (247,358 atoms, total time ∼ 4.4 μs), we demonstrate, for the first time, that the kinesin-1 motor domain can be detached from a microtubule by an intense electric field within the nanosecond timescale. We show that this effect is field-direction dependent and field-strength dependent. A detailed analysis of the electric forces and the work carried out by electric field acting on the microtubule–kinesin system shows that it is the combined action of the electric field pulling on the β-tubulin C-terminus and the electric-field-induced torque on the kinesin dipole moment that causes kinesin detachment from the microtubule. It is shown, for the first time in a mechanistic manner, that an electric field can dramatically affect molecular interactions in a heterologous functional protein assembly. Our results contribute to understanding of electromagnetic field–biomatter interactions on a molecular level, with potential biomedical and bio-nanotechnological applications for harnessing control of protein nanomotors.http://www.sciencedirect.com/science/article/pii/S2001037023000193Electric fieldProteinsTubulinMicrotubulesMolecular dynamics simulation |
| spellingShingle | Jiří Průša Michal Cifra Electro-detachment of kinesin motor domain from microtubule in silico Computational and Structural Biotechnology Journal Electric field Proteins Tubulin Microtubules Molecular dynamics simulation |
| title | Electro-detachment of kinesin motor domain from microtubule in silico |
| title_full | Electro-detachment of kinesin motor domain from microtubule in silico |
| title_fullStr | Electro-detachment of kinesin motor domain from microtubule in silico |
| title_full_unstemmed | Electro-detachment of kinesin motor domain from microtubule in silico |
| title_short | Electro-detachment of kinesin motor domain from microtubule in silico |
| title_sort | electro detachment of kinesin motor domain from microtubule in silico |
| topic | Electric field Proteins Tubulin Microtubules Molecular dynamics simulation |
| url | http://www.sciencedirect.com/science/article/pii/S2001037023000193 |
| work_keys_str_mv | AT jiriprusa electrodetachmentofkinesinmotordomainfrommicrotubuleinsilico AT michalcifra electrodetachmentofkinesinmotordomainfrommicrotubuleinsilico |