Mercury and Alzheimer's Disease: Hg(II) Ions Display Specific Binding to the Amyloid-β Peptide and Hinder Its Fibrillization.
Clicks: 364
ID: 74214
2019
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This
article has not been analysed, so there is no overall score —
reader engagement is measured and shown alongside.
Reader Engagement
Steady Performance
68.4
/100
364 views
235 readers
Trending
AI Quality Assessment
Not analyzed
Readership in this journal
SteadyRanked #16 of 99 articles by views in Biomolecules
Most read
Least read
Bar heights use a square-root scale.
Mint this article as an NFT
Not yet mintedCreate a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.
5
SUSD
one-off · no wallet required
Abstract
Brains and blood of Alzheimer's disease (AD) patients have shown elevated mercury concentrations, but potential involvement of mercury exposure in AD pathogenesis has not been studied at the molecular level. The pathological hallmark of AD brains is deposition of amyloid plaques, consisting mainly of amyloid-β (Aβ) peptides aggregated into amyloid fibrils. Aβ peptide fibrillization is known to be modulated by metal ions such as Cu(II) and Zn(II). Here, we study in vitro the interactions between Aβ peptides and Hg(II) ions by multiple biophysical techniques. Fluorescence spectroscopy and atomic force microscopy (AFM) show that Hg(II) ions have a concentration-dependent inhibiting effect on Aβ fibrillization: at a 1:1 Aβ·Hg(II) ratio only non-fibrillar Aβ aggregates are formed. NMR spectroscopy shows that Hg(II) ions interact with the N-terminal region of Aβ(1-40) with a micromolar affinity, likely via a binding mode similar to that for Cu(II) and Zn(II) ions, i.e., mainly via the histidine residues His6, His13, and His14. Thus, together with Cu(II), Fe(II), Mn(II), Pb(IV), and Zn(II) ions, Hg(II) belongs to a family of metal ions that display residue-specific binding interactions with Aβ peptides and modulate their aggregation processes.
| Reference Key |
wallin2019mercurybiomolecules
Use this key to autocite in the manuscript while using
SciMatic Manuscript Manager or Thesis Manager
|
|---|---|
| Authors | Wallin, Cecilia;Friedemann, Merlin;Sholts, Sabrina B;Noormägi, Andra;Svantesson, Teodor;Jarvet, Jüri;Roos, Per M;Palumaa, Peep;Gräslund, Astrid;Wärmländer, Sebastian K T S; |
| Journal | Biomolecules |
| Year | 2019 |
| DOI |
E44
|
| URL | |
| Keywords |
mercury
alzheimer’s disease
neurodegeneration
amyloid aggregation
metal–protein binding
eugenol
renewable resources
thermosets
Screening
Education
stroke
sickle cell disease
transcranial doppler (tcd)
eudragit® s100
hiv sexual transmission
tenofovir controlled release
chitosan citrate
chitosan lactate
chitosan tartrate
layer-by-layer film
mucoadhesive film
ph responsive release
vaginal preexposure prophylaxis
Evaluation
behaviour change
primary care
self-care
general practice
antibiotic pharmacist
|
Citations
No citations found. To add a citation, contact the admin at info@scimatic.org
Comments
No comments yet. Be the first to comment on this article.