Crystal structures of human serum albumin in complex with lysophosphatidylcholine.
Journal
Biophysical journal
ISSN: 1542-0086
Titre abrégé: Biophys J
Pays: United States
ID NLM: 0370626
Informations de publication
Date de publication:
07 11 2023
07 11 2023
Historique:
received:
07
07
2023
revised:
04
09
2023
accepted:
14
09
2023
pmc-release:
07
11
2024
medline:
10
11
2023
pubmed:
21
9
2023
entrez:
21
9
2023
Statut:
ppublish
Résumé
Lysophospholipids (lysoPLs) are crucial metabolites involved in various physiological and pathological cellular processes. Understanding their binding interactions, particularly with human serum albumin (HSA), is essential due to their role in regulating lysoPLs-induced cytotoxicity. However, the precise mechanism of lysoPLs binding to HSA remains elusive. In this study, we employed fluorescence quenching and optical interferometry assays to demonstrate direct binding between lysophosphatidylcholine (LPC) and HSA (K
Identifiants
pubmed: 37731243
pii: S0006-3495(23)00584-2
doi: 10.1016/j.bpj.2023.09.007
pmc: PMC10645546
pii:
doi:
Substances chimiques
Serum Albumin, Human
ZIF514RVZR
Lysophosphatidylcholines
0
Serum Albumin
0
Myristates
0
Fatty Acids
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4135-4143Informations de copyright
Copyright © 2023 Biophysical Society. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.
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