Molecular displacement of warfarin from human serum albumin by flavonoid aglycones

Miklós Poór, Yin Li, S. Kunsági-Máté, József Petrik, Sanda Vladimir-Knežević, T. Kőszegi

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

The well-known 4-hydroxycoumarin derivative warfarin is a widespread anticoagulant drug. Besides its strong albumin binding property warfarin has a narrow therapeutic window. Therefore, a few percent of displacement from albumin can result in serious biological consequences. The flavonoid molecular group also shows very strong plasma albumin binding characteristics occupying the same binding site. It is plausible to hypothesize that flavonoid aglycones may be able to displace warfarin from human serum albumin (HSA). In our study the competing activities of different flavone (acacetin, apigenin, chrysin, luteolin), flavonol (galangin, quercetin) and flavanone (hesperetin, naringenin) aglycones were investigated using fluorescence spectroscopy. Our results represent that flavonoids are able to displace warfarin from the surface of HSA. On the other hand, when comparing flavone or flavonol groups to flavanones the latter group seems to be much weaker competitor. These observations were also supported by calculation of stability constants. Our investigations strongly suggest that we should reckon with the described molecular displacement. However, further in vivo studies are needed to support the findings of our model system.

Original languageEnglish
Pages (from-to)122-127
Number of pages6
JournalJournal of Luminescence
Volume142
DOIs
Publication statusPublished - 2013

Fingerprint

flavone
Warfarin
albumins
Flavonoids
Serum Albumin
serums
Albumins
Flavanones
Apigenin
Luteolin
anticoagulants
Fluorescence Spectrometry
Quercetin
Fluorescence spectroscopy
Anticoagulants
Binding Sites
Derivatives
drugs
fluorescence
spectroscopy

Keywords

  • Flavonoid aglycones
  • Fluorescence spectroscopy
  • Human serum albumin
  • Molecular displacement
  • Warfarin

ASJC Scopus subject areas

  • Atomic and Molecular Physics, and Optics
  • Condensed Matter Physics
  • Chemistry(all)
  • Biochemistry
  • Biophysics

Cite this

Molecular displacement of warfarin from human serum albumin by flavonoid aglycones. / Poór, Miklós; Li, Yin; Kunsági-Máté, S.; Petrik, József; Vladimir-Knežević, Sanda; Kőszegi, T.

In: Journal of Luminescence, Vol. 142, 2013, p. 122-127.

Research output: Contribution to journalArticle

Poór, Miklós ; Li, Yin ; Kunsági-Máté, S. ; Petrik, József ; Vladimir-Knežević, Sanda ; Kőszegi, T. / Molecular displacement of warfarin from human serum albumin by flavonoid aglycones. In: Journal of Luminescence. 2013 ; Vol. 142. pp. 122-127.
@article{a41e1b4e48a2424ba167b234ad6f85f5,
title = "Molecular displacement of warfarin from human serum albumin by flavonoid aglycones",
abstract = "The well-known 4-hydroxycoumarin derivative warfarin is a widespread anticoagulant drug. Besides its strong albumin binding property warfarin has a narrow therapeutic window. Therefore, a few percent of displacement from albumin can result in serious biological consequences. The flavonoid molecular group also shows very strong plasma albumin binding characteristics occupying the same binding site. It is plausible to hypothesize that flavonoid aglycones may be able to displace warfarin from human serum albumin (HSA). In our study the competing activities of different flavone (acacetin, apigenin, chrysin, luteolin), flavonol (galangin, quercetin) and flavanone (hesperetin, naringenin) aglycones were investigated using fluorescence spectroscopy. Our results represent that flavonoids are able to displace warfarin from the surface of HSA. On the other hand, when comparing flavone or flavonol groups to flavanones the latter group seems to be much weaker competitor. These observations were also supported by calculation of stability constants. Our investigations strongly suggest that we should reckon with the described molecular displacement. However, further in vivo studies are needed to support the findings of our model system.",
keywords = "Flavonoid aglycones, Fluorescence spectroscopy, Human serum albumin, Molecular displacement, Warfarin",
author = "Mikl{\'o}s Po{\'o}r and Yin Li and S. Kuns{\'a}gi-M{\'a}t{\'e} and J{\'o}zsef Petrik and Sanda Vladimir-Knežević and T. Kőszegi",
year = "2013",
doi = "10.1016/j.jlumin.2013.03.056",
language = "English",
volume = "142",
pages = "122--127",
journal = "Journal of Luminescence",
issn = "0022-2313",
publisher = "Elsevier",

}

TY - JOUR

T1 - Molecular displacement of warfarin from human serum albumin by flavonoid aglycones

AU - Poór, Miklós

AU - Li, Yin

AU - Kunsági-Máté, S.

AU - Petrik, József

AU - Vladimir-Knežević, Sanda

AU - Kőszegi, T.

PY - 2013

Y1 - 2013

N2 - The well-known 4-hydroxycoumarin derivative warfarin is a widespread anticoagulant drug. Besides its strong albumin binding property warfarin has a narrow therapeutic window. Therefore, a few percent of displacement from albumin can result in serious biological consequences. The flavonoid molecular group also shows very strong plasma albumin binding characteristics occupying the same binding site. It is plausible to hypothesize that flavonoid aglycones may be able to displace warfarin from human serum albumin (HSA). In our study the competing activities of different flavone (acacetin, apigenin, chrysin, luteolin), flavonol (galangin, quercetin) and flavanone (hesperetin, naringenin) aglycones were investigated using fluorescence spectroscopy. Our results represent that flavonoids are able to displace warfarin from the surface of HSA. On the other hand, when comparing flavone or flavonol groups to flavanones the latter group seems to be much weaker competitor. These observations were also supported by calculation of stability constants. Our investigations strongly suggest that we should reckon with the described molecular displacement. However, further in vivo studies are needed to support the findings of our model system.

AB - The well-known 4-hydroxycoumarin derivative warfarin is a widespread anticoagulant drug. Besides its strong albumin binding property warfarin has a narrow therapeutic window. Therefore, a few percent of displacement from albumin can result in serious biological consequences. The flavonoid molecular group also shows very strong plasma albumin binding characteristics occupying the same binding site. It is plausible to hypothesize that flavonoid aglycones may be able to displace warfarin from human serum albumin (HSA). In our study the competing activities of different flavone (acacetin, apigenin, chrysin, luteolin), flavonol (galangin, quercetin) and flavanone (hesperetin, naringenin) aglycones were investigated using fluorescence spectroscopy. Our results represent that flavonoids are able to displace warfarin from the surface of HSA. On the other hand, when comparing flavone or flavonol groups to flavanones the latter group seems to be much weaker competitor. These observations were also supported by calculation of stability constants. Our investigations strongly suggest that we should reckon with the described molecular displacement. However, further in vivo studies are needed to support the findings of our model system.

KW - Flavonoid aglycones

KW - Fluorescence spectroscopy

KW - Human serum albumin

KW - Molecular displacement

KW - Warfarin

UR - http://www.scopus.com/inward/record.url?scp=84877326435&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84877326435&partnerID=8YFLogxK

U2 - 10.1016/j.jlumin.2013.03.056

DO - 10.1016/j.jlumin.2013.03.056

M3 - Article

VL - 142

SP - 122

EP - 127

JO - Journal of Luminescence

JF - Journal of Luminescence

SN - 0022-2313

ER -