Electro-detachment of kinesin motor domain from microtubule in silico

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985882%3A_____%2F23%3A00570259" target="_blank" >RIV/67985882:_____/23:00570259 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.csbj.2023.01.018" target="_blank" >http://dx.doi.org/10.1016/j.csbj.2023.01.018</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.csbj.2023.01.018" target="_blank" >10.1016/j.csbj.2023.01.018</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Electro-detachment of kinesin motor domain from microtubule in silico

Popis výsledku v původním jazyce

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 cir-cumvent 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 mu s), 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 fielddirection 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-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.(c) 2023 The Author(s). Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology. This is an open access article under the CC BY-NC-ND license (http://creative-commons.org/licens es/by-nc-nd/4.0/)

Název v anglickém jazyce

Electro-detachment of kinesin motor domain from microtubule in silico

Popis výsledku anglicky

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 cir-cumvent 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 mu s), 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 fielddirection 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-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.(c) 2023 The Author(s). Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology. This is an open access article under the CC BY-NC-ND license (http://creative-commons.org/licens es/by-nc-nd/4.0/)

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10610 - Biophysics

Projekt

<a href="/cs/project/GX20-06873X" target="_blank" >GX20-06873X: SubTHz chipová zařízení pro řízení proteinových nanopřístrojů</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2023

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Computational and Structural Biotechnology Journal

ISSN

2001-0370

e-ISSN

2001-0370

Svazek periodika

21

Číslo periodika v rámci svazku

FEB 2023

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

13

Strana od-do

1349-1361

Kód UT WoS článku

000933953200001

EID výsledku v databázi Scopus

2-s2.0-85147798567