Characterisation of the binding of dihydro-alpha-lipoic acid to fibrinogen and the effects on fibrinogen oxidation and fibrin formation.
Molecular modelling
Protein function
Protein interaction
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
15 Mar 2020
15 Mar 2020
Historique:
received:
05
11
2019
revised:
08
01
2020
accepted:
09
01
2020
pubmed:
14
1
2020
medline:
28
11
2020
entrez:
14
1
2020
Statut:
ppublish
Résumé
A reduced form of the alpha-lipoic acid, dihydro-alpha-lipoic acid (DHLA) is a potent, naturally occurring antioxidant which can be consumed as food constituent or as supplement at doses up to 600 mg/day. DHLA has inhibitory effect on coagulation as it can reduce concentrations of some coagulation factors. In this study, a direct interaction between DHLA and fibrinogen, the main protein in coagulation, is described. Binding constant for DHLA/fibrinogen complex is of moderate strength (10
Identifiants
pubmed: 31931063
pii: S0141-8130(19)39010-5
doi: 10.1016/j.ijbiomac.2020.01.098
pii:
doi:
Substances chimiques
Antioxidants
0
Thioctic Acid
73Y7P0K73Y
Fibrin
9001-31-4
Fibrinogen
9001-32-5
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
319-325Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.