Metal Ion Binding of Vimentin Tail Domain Fragments
Carranza EJ., Heffern MC., Murray DT.
Laboratory Study, published in Chembiochem (2026) — summary generated from the PubMed abstract.
Evidence from laboratory and animal studies provides groundwork for understanding mechanisms and potential before human studies continue.
- Level A · Stronger Clinical Evidence
- Level B · Emerging clinical evidence with positive signals
- Level C · Early human research exploring benefits
- Level D · Scientific groundwork from lab and animal studies
- Emerging · Emerging topic under active research
This page is generated from the PubMed record. The Thai description is an automated summary of bibliographic fields and the abstract, not a full translation, and is not medical advice.
- Study type
- Laboratory Study
- Journal
- Chembiochem (2026)
- Reported sample size
- —
- Source database
- Europe PMC
- PMID
- 42054155
- PMCID
- PMC13127699
- DOI
- 10.1002/cbic.70353
Abstract (original English)
The intermediate filament (IF) protein vimentin is a critical component of the cell cytoskeleton, yet our mechanistic understanding of head and tail domain function is incomplete. The C-terminal tail domain of vimentin is of increasing interest as it is essential for regulating the structure and mechanical properties of filament networks through interactions with divalent metal ions. However, the molecular basis of tail domain-metal interactions has not been characterized. Here, we analyze the structural and metal-binding properties of the vimentin tail domain. Mass spectrometry, UV-vis, and circular dichroism (CD) spectroscopy reveal binding of divalent copper (Cu(II)) to both a peptide composed of the last 11 residues of the tail domain and the complete, isolated tail domain. Solution nuclear magnetic resonance and CD measurements show that in the absence of Cu(II), the complete vimentin tail domain is primarily disordered and that Cu(II)-binding involves both the last 11 residues and another segment in the middle of the tail domain, leaving the N-terminal portion of the tail domain primarily disordered. Our study provides a Cu(II) binding model for the isolated vimentin tail domain that can assist with the interpretation of Cu(II) mediated effects on vimentin structure in biological contexts.
What this study does not prove
- • This study does not prove SVF is an approved treatment or a replacement for standard care.
- • This is preclinical work; animal or laboratory results cannot be applied to humans.
Evidence level
Evidence from laboratory and animal studies provides groundwork for understanding mechanisms and potential before human studies continue.
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