prikaz prve stranice dokumenta Warfarin and Flavonoids do not Share the Same Binding Region in Binding to the IIA Subdomain of Human Serum Albumin
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Warfarin and Flavonoids do not Share the Same Binding Region in Binding to the IIA Subdomain of Human Serum Albumin
Molecules, 22 (2017), 7; 2-14. https://doi.org/10.3390/molecules22071153
Rimac, Hrvoje; Dufour, Claire; Debeljak, Željko; Zorc, Branka; Bojić, Mirza

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Rimac, H., Dufour, C., Debeljak, Ž., Zorc, B. & Bojić, M. (2017). Warfarin and Flavonoids do not Share the Same Binding Region in Binding to the IIA Subdomain of Human Serum Albumin. Molecules, 22. (7), 2-14. doi: 10.3390/molecules22071153

Rimac, Hrvoje, et al. "Warfarin and Flavonoids do not Share the Same Binding Region in Binding to the IIA Subdomain of Human Serum Albumin." Molecules, vol. 22, no. 7, 2017, pp. 2-14. https://doi.org/10.3390/molecules22071153

Rimac, Hrvoje, Claire Dufour, Željko Debeljak, Branka Zorc and Mirza Bojić. "Warfarin and Flavonoids do not Share the Same Binding Region in Binding to the IIA Subdomain of Human Serum Albumin." Molecules 22, no. 7 (2017): 2-14. https://doi.org/10.3390/molecules22071153

Rimac, H., et al. (2017) 'Warfarin and Flavonoids do not Share the Same Binding Region in Binding to the IIA Subdomain of Human Serum Albumin', Molecules, 22(7), pp. 2-14. doi: 10.3390/molecules22071153

Rimac H, Dufour C, Debeljak Ž, Zorc B, Bojić M. Warfarin and Flavonoids do not Share the Same Binding Region in Binding to the IIA Subdomain of Human Serum Albumin. Molecules [Internet]. 2017 [cited 2024 November 16];22(7):2-14. doi: 10.3390/molecules22071153

H. Rimac, C. Dufour, Ž. Debeljak, B. Zorc and M. Bojić, "Warfarin and Flavonoids do not Share the Same Binding Region in Binding to the IIA Subdomain of Human Serum Albumin", Molecules, vol. 22, no. 7, pp. 2-14, 2017. [Online]. Available at: https://urn.nsk.hr/urn:nbn:hr:239:860737. [Accessed: 16 November 2024]

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Metadata
Title (english)Warfarin and Flavonoids do not Share the Same Binding Region in Binding to the IIA Subdomain of Human Serum Albumin
AuthorHrvoje Rimac
MBZ: 335535
AuthorClaire Dufour
AuthorŽeljko Debeljak
MBZ: 296571
AuthorBranka Zorc
MBZ: 80914
AuthorMirza Bojić
MBZ: 298301
Author's institution(Clinical hospital center Osijek)
Author's institutionJosip Juraj Strossmayer University of Osijek
Faculty of Medicine Osijek
Author's institutionUniversity of Zagreb
Faculty of Pharmacy and Biochemistry
Scientific / art field,
discipline and subdiscipline		BIOMEDICINE AND HEALTHCARE
Pharmacy
Medical Biochemistry
Scientific / art field,
discipline and subdiscipline		BIOMEDICINE AND HEALTHCARE
Basic Medical Sciences
Pharmacology
Abstract (english)
Human serum albumin (HSA) binds a variety of xenobiotics, including flavonoids and warfarin. The binding of another ligand to the IIA binding site on HSA can cause warfarin displacement and potentially the elevation of its free concentration in blood. Studies dealing with flavonoid-induced warfarin displacement from HSA provided controversial results: estimated risk of displacement ranged from none to serious. To resolve these controversies, in vitro study of simultaneous binding of warfarin and eight different flavonoid aglycons and glycosides to HSA was carried out by fluorescence spectroscopy as well as molecular docking. Results show that warfarin and flavonoids do not share the same binding region in binding to HSA. Interactions were only observed at high warfarin concentrations not attainable under recommended dosing regimes. Docking experiments show that flavonoid aglycons and glycosides do not bind at warfarin high affinity sites, but rather to different regions within the IIA HSA subdomain. Thus, the risk of clinically significant warfarin-flavonoid interaction in binding to HSA should be regarded as negligible.
Keywords (english)
Languageenglish
Publication typeProfessional paper - Professional paper
Publication statusPublished
Peer reviewPeer review - international
Publication versionPublished version
Journal titleMolecules
Numberingvol. 22, no. 7, pp. 2-14
e-ISSN1420-3049
DOIhttps://doi.org/10.3390/molecules22071153
URN:NBNurn:nbn:hr:239:860737
Publication2017
Document URLhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6152318/
Type of resourceText
Access conditionsOpen access
Terms of useLicence Attribution 4.0 International (CC BY 4.0) icon
Created on2020-05-04 09:40:40