The Transthyretin/Oleuropein Aglycone Complex: A New Tool against TTR Amyloidosis.
misfolding
polyphenols
systemic amyloidosis
transthyretin
Journal
Pharmaceuticals (Basel, Switzerland)
ISSN: 1424-8247
Titre abrégé: Pharmaceuticals (Basel)
Pays: Switzerland
ID NLM: 101238453
Informations de publication
Date de publication:
23 Feb 2022
23 Feb 2022
Historique:
received:
26
01
2022
revised:
17
02
2022
accepted:
21
02
2022
entrez:
26
3
2022
pubmed:
27
3
2022
medline:
27
3
2022
Statut:
epublish
Résumé
The release of monomers from the homotetrameric protein transthyretin (TTR) is the first event of a cascade, eventually leading to sporadic or familial TTR amyloidoses. Thus, ligands able to stabilize TTR and inhibit monomer release are subject of intense scrutiny as potential treatments against these pathologies. Here, we investigated the interaction between TTR and a non-glycated derivative of the main olive polyphenol, oleuropein (OleA), known to interfere with TTR aggregation. We coupled fluorescence studies with molecular docking to investigate the OleA/TTR interaction using wild-type TTR, a monomeric variant, and the L55P cardiotoxic mutant. We characterized a fluorescence band emitted by OleA upon formation of the OleA/TTR complex. Exploiting this signal, we found that a poorly specific non-stoichiometric interaction occurs on the surface of the protein and a more specific stabilizing interaction takes place in the ligand binding pocket of TTR, exhibiting a
Identifiants
pubmed: 35337074
pii: ph15030277
doi: 10.3390/ph15030277
pmc: PMC8953266
pii:
doi:
Types de publication
Journal Article
Langues
eng
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