Binding of direct oral anticoagulants to the FA1 site of human serum albumin.
competitive inhibition of heme binding
direct oral anticoagulants
human serum albumin
human serum albumin:direct oral anticoagulant recognition
molecular docking
Journal
Journal of molecular recognition : JMR
ISSN: 1099-1352
Titre abrégé: J Mol Recognit
Pays: England
ID NLM: 9004580
Informations de publication
Date de publication:
03 2021
03 2021
Historique:
received:
27
03
2020
revised:
07
09
2020
accepted:
11
09
2020
pubmed:
10
10
2020
medline:
1
2
2022
entrez:
9
10
2020
Statut:
ppublish
Résumé
The anticoagulant therapy is widely used to prevent and treat thromboembolic events. Until the last decade, vitamin K antagonists were the only available oral anticoagulants; recently, direct oral anticoagulants (DOACs) have been developed. Since 55% to 95% of DOACs are bound to plasma proteins, the in silico docking and ligand-binding properties of drugs apixaban, betrixaban, dabigatran, edoxaban, and rivaroxaban and of the prodrug dabigatran etexilate to human serum albumin (HSA), the most abundant plasma protein, have been investigated. DOACs bind to the fatty acid (FA) site 1 (FA1) of ligand-free HSA, whereas they bind to the FA8 and FA9 sites of heme-Fe(III)- and myristic acid-bound HSA. DOACs binding to the FA1 site of ligand-free HSA has been validated by competitive inhibition of heme-Fe(III) recognition. Values of the dissociation equilibrium constant for DOACs binding to the FA1 site (ie,
Substances chimiques
Factor Xa Inhibitors
0
Fatty Acids
0
Rivaroxaban
9NDF7JZ4M3
Serum Albumin, Human
ZIF514RVZR
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2877Informations de copyright
© 2020 John Wiley & Sons Ltd.
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