Plumbagin accelerates serum albumin amyloid aggregation kinetics and generates fibril polymorphism by inducing non-native β-sheet structures.
Amyloid fibrils
Biophysical chemistry
Conformational switch
Ligand-protein binding
Journal
Biochimica et biophysica acta. Proteins and proteomics
ISSN: 1878-1454
Titre abrégé: Biochim Biophys Acta Proteins Proteom
Pays: Netherlands
ID NLM: 101731734
Informations de publication
Date de publication:
05 Jun 2024
05 Jun 2024
Historique:
received:
08
03
2024
revised:
31
05
2024
accepted:
03
06
2024
medline:
8
6
2024
pubmed:
8
6
2024
entrez:
7
6
2024
Statut:
aheadofprint
Résumé
The ligand-induced conformational switch of proteins has great significance in understanding the biophysics and biochemistry of their self-assembly. In this work, we have investigated the ability of plumbagin (PL), a hydroxynaphthoquinone compound found in the root of the medicinal plant Plumbago zeylanica, to modulate aggregation precursor state, aggregation kinetics and generate distinct fibril of human serum albumin (HSA). PL was found to moderately bind (binding constant K
Identifiants
pubmed: 38849109
pii: S1570-9639(24)00035-9
doi: 10.1016/j.bbapap.2024.141028
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
141028Informations de copyright
Copyright © 2024. Published by Elsevier B.V.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.