Mechanical characterization of spectrin at the molecular level.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
18 Jul 2024
18 Jul 2024
Historique:
received:
18
02
2024
accepted:
11
07
2024
medline:
19
7
2024
pubmed:
19
7
2024
entrez:
18
7
2024
Statut:
epublish
Résumé
Spectrin, a large cytoskeletal protein, consists of a heterodimeric structure comprising α and β subunits. Here, we have studied the mechanics of spectrin filament as a major constituent of dendrites and dendritic spines. Given the intricate biological details and compact biological construction of spectrin, we've developed a constitutive model of spectrin that describes its continuous deformation over three distinct stages and it's progressive failure mechanisms. Our model closely predicts both the force at which uncoiling begins and the ultimate force at which spectrin fails, measuring approximately 93 ~ 100 pN. Remarkably, our predicted failure force closely matches the findings from AFM experiments focused on the uncoiling of spectrin repeats, which reported a force of 90 pN. Our theoretical model proposes a plausible pathway for the potential failure of dendrites and the intricate connection between strain and strain rate. These findings deepen our understanding of how spectrin can contribute to traumatic brain injury risk analysis.
Identifiants
pubmed: 39025938
doi: 10.1038/s41598-024-67500-0
pii: 10.1038/s41598-024-67500-0
doi:
Substances chimiques
Spectrin
12634-43-4
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
16631Subventions
Organisme : Office of Naval Research
ID : N00014-21-1-2855(0000001556)
Organisme : Office of Naval Research
ID : N00014-21-1-2855(0000001556)
Informations de copyright
© 2024. The Author(s).
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