Ibuprofen Favors Binding of Amyloid-β Peptide to Its Depot, Serum Albumin.


Journal

International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791

Informations de publication

Date de publication:
31 May 2022
Historique:
received: 15 04 2022
revised: 24 05 2022
accepted: 28 05 2022
entrez: 10 6 2022
pubmed: 11 6 2022
medline: 14 6 2022
Statut: epublish

Résumé

The deposition of amyloid-β peptide (Aβ) in the brain is a critical event in the progression of Alzheimer's disease (AD). This Aβ deposition could be prevented by directed enhancement of Aβ binding to its natural depot, human serum albumin (HSA). Previously, we revealed that specific endogenous ligands of HSA improve its affinity to monomeric Aβ. We show here that an exogenous HSA ligand, ibuprofen (IBU), exerts the analogous effect. Plasmon resonance spectroscopy data evidence that a therapeutic IBU level increases HSA affinity to monomeric Aβ

Identifiants

pubmed: 35682848
pii: ijms23116168
doi: 10.3390/ijms23116168
pmc: PMC9181795
pii:
doi:

Substances chimiques

Amyloid beta-Peptides 0
Ligands 0
Peptide Fragments 0
Serum Albumin 0
Ibuprofen WK2XYI10QM
Serum Albumin, Human ZIF514RVZR

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Russian Science Foundation
ID : 20-74-10072

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Auteurs

Ekaterina A Litus (EA)

Institute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.

Alexey S Kazakov (AS)

Institute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.

Evgenia I Deryusheva (EI)

Institute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.

Ekaterina L Nemashkalova (EL)

Institute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.

Marina P Shevelyova (MP)

Institute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.

Andrey V Machulin (AV)

Skryabin Institute of Biochemistry and Physiology of Microorganisms, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.

Aliya A Nazipova (AA)

Institute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.

Maria E Permyakova (ME)

Institute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.

Vladimir N Uversky (VN)

Department of Molecular Medicine, Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA.

Sergei E Permyakov (SE)

Institute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.

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Classifications MeSH