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Atomistic Modeling of F-Actin Mechanical Responses and Determination of Mechanical Properties

Si Li, Jin Zhang, Chengyuan Wang Orcid Logo, Perumal Nithiarasu

ACS Biomaterials Science & Engineering, Volume: 4, Issue: 8, Pages: 2794 - 2803

Swansea University Author: Chengyuan Wang Orcid Logo

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DOI (Published version): 10.1021/acsbiomaterials.8b00640

Abstract

A molecular structural mechanics (MSM) model was developed for F-actins in cells, where the force constants describing the monomer interaction were achieved using molecular dynamics simulations. The MSM was then employed to predict the mechanical properties of F-actin. The obtained Young’s modulus (...

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Published in: ACS Biomaterials Science & Engineering
ISSN: 2373-9878 2373-9878
Published: 2018
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URI: https://cronfa.swan.ac.uk/Record/cronfa40781
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first_indexed 2018-06-21T13:26:51Z
last_indexed 2018-09-10T12:55:49Z
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spelling 2018-09-10T10:19:46.0082800 v2 40781 2018-06-21 Atomistic Modeling of F-Actin Mechanical Responses and Determination of Mechanical Properties fdea93ab99f51d0b3921d3601876c1e5 0000-0002-1001-2537 Chengyuan Wang Chengyuan Wang true false 2018-06-21 MECH A molecular structural mechanics (MSM) model was developed for F-actins in cells, where the force constants describing the monomer interaction were achieved using molecular dynamics simulations. The MSM was then employed to predict the mechanical properties of F-actin. The obtained Young’s modulus (1.92 GPa), torsional rigidity (2.36 × 10–26 Nm2), and flexural rigidity (10.84 × 10–26 Nm2) were found to be in good agreement with existing experimental data. Subsequently, the tension-induced bending was studied for F-actins as a result of their helical structure. Mechanical instability was also investigated for the actin filaments in filopodial protrusion by considering the reinforcing effect of the actin-binding proteins. The predicted buckling load agreed well with the experimentally obtained stall force, showing a pivotal role of the actin-binding protein in regulating the stiffness of F-actin bundles during the formation of filopodia protrusion. Herein, it is expected that the MSM model can be extended to the mechanics of more complex filamentous systems such as stress fibers and actin meshwork. Journal Article ACS Biomaterials Science & Engineering 4 8 2794 2803 2373-9878 2373-9878 actin filament; molecular dynamics simulations; molecular mechanics; structural details; structural mechanics model 31 12 2018 2018-12-31 10.1021/acsbiomaterials.8b00640 COLLEGE NANME Mechanical Engineering COLLEGE CODE MECH Swansea University 2018-09-10T10:19:46.0082800 2018-06-21T08:59:26.0686363 Si Li 1 Jin Zhang 2 Chengyuan Wang 0000-0002-1001-2537 3 Perumal Nithiarasu 4 0040781-21062018090129.pdf li2018(6).pdf 2018-06-21T09:01:29.1870000 Output 2287251 application/pdf Accepted Manuscript true 2019-06-19T00:00:00.0000000 true eng
title Atomistic Modeling of F-Actin Mechanical Responses and Determination of Mechanical Properties
spellingShingle Atomistic Modeling of F-Actin Mechanical Responses and Determination of Mechanical Properties
Chengyuan Wang
title_short Atomistic Modeling of F-Actin Mechanical Responses and Determination of Mechanical Properties
title_full Atomistic Modeling of F-Actin Mechanical Responses and Determination of Mechanical Properties
title_fullStr Atomistic Modeling of F-Actin Mechanical Responses and Determination of Mechanical Properties
title_full_unstemmed Atomistic Modeling of F-Actin Mechanical Responses and Determination of Mechanical Properties
title_sort Atomistic Modeling of F-Actin Mechanical Responses and Determination of Mechanical Properties
author_id_str_mv fdea93ab99f51d0b3921d3601876c1e5
author_id_fullname_str_mv fdea93ab99f51d0b3921d3601876c1e5_***_Chengyuan Wang
author Chengyuan Wang
author2 Si Li
Jin Zhang
Chengyuan Wang
Perumal Nithiarasu
format Journal article
container_title ACS Biomaterials Science & Engineering
container_volume 4
container_issue 8
container_start_page 2794
publishDate 2018
institution Swansea University
issn 2373-9878
2373-9878
doi_str_mv 10.1021/acsbiomaterials.8b00640
document_store_str 1
active_str 0
description A molecular structural mechanics (MSM) model was developed for F-actins in cells, where the force constants describing the monomer interaction were achieved using molecular dynamics simulations. The MSM was then employed to predict the mechanical properties of F-actin. The obtained Young’s modulus (1.92 GPa), torsional rigidity (2.36 × 10–26 Nm2), and flexural rigidity (10.84 × 10–26 Nm2) were found to be in good agreement with existing experimental data. Subsequently, the tension-induced bending was studied for F-actins as a result of their helical structure. Mechanical instability was also investigated for the actin filaments in filopodial protrusion by considering the reinforcing effect of the actin-binding proteins. The predicted buckling load agreed well with the experimentally obtained stall force, showing a pivotal role of the actin-binding protein in regulating the stiffness of F-actin bundles during the formation of filopodia protrusion. Herein, it is expected that the MSM model can be extended to the mechanics of more complex filamentous systems such as stress fibers and actin meshwork.
published_date 2018-12-31T03:51:55Z
_version_ 1763752558692663296
score 11.035655

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