Structural characterization of fondaparinux interaction with per-6-amino-beta-cyclodextrin: An NMR and MS study.
Antidote
Degradation
Electrostatic interaction
Heparin
NMR
Journal
Journal of pharmaceutical and biomedical analysis
ISSN: 1873-264X
Titre abrégé: J Pharm Biomed Anal
Pays: England
ID NLM: 8309336
Informations de publication
Date de publication:
15 Apr 2021
15 Apr 2021
Historique:
received:
16
10
2020
revised:
28
01
2021
accepted:
30
01
2021
pubmed:
19
2
2021
medline:
22
6
2021
entrez:
18
2
2021
Statut:
ppublish
Résumé
The highly anionic synthetic pentasaccharide fondaparinux (FDPX) - representing the antithrombin binding sequence of heparin - is in clinical use as a potent anticoagulant. Contrary to the unfractionated heparin, FDPX lacks potent antidote completely reversing its anticoagulant activity, therefore it is of great importance to identify new structures exhibiting strong intermolecular interactions towards FDPX. The polycationic heptakis(6-amino-6-deoxy)-beta-cyclodextrin (NH
Identifiants
pubmed: 33601159
pii: S0731-7085(21)00059-5
doi: 10.1016/j.jpba.2021.113947
pii:
doi:
Substances chimiques
beta-Cyclodextrins
0
per-6-amino-beta-cyclodextrin
0
Heparin
9005-49-6
Fondaparinux
J177FOW5JL
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
113947Informations de copyright
Copyright © 2021 The Author(s). Published by Elsevier B.V. All rights reserved.
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.