Protoapigenone derivatives: Albumin binding properties and effects on HepG2 cells

Miklós Poór, Yin Li, S. Kunsági-Máté, Zsófia Varga, Attila Hunyadi, Balázs Dankó, Fang Rong Chang, Yang Chang Wu, T. Kőszegi

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Protoapigenone (Pa) is a flavone aglycone with a p-quinol structure in its B-ring. It was first discovered in Thelypteris torresiana, a native fern in Taiwan. Recent studies highlighted that protoapigenone and some of its derivatives show very potent anticancer activity against several types of tumors, using both in vitro and in vivo models. Despite the growing body of evidence on the selective anticancer potential of protoapigenone and its derivatives, no data are available on their pharmacokinetical properties. In our present research, albumin binding properties of Pa and seven different 1′-O-alkyl protoapigenone derivatives were analyzed as well as their biochemical effects on HepG2 tumor cell line in comparison with the flavone apigenin. Our results are in good accordance with the data of previous investigations of 1′-O-alkylated derivatives of protoapigenone (with the exception of isopropyl and allyl derivatives) showing similar or higher antitumor effects than Pa. Furthermore structural changes in Pa cause a very remarkable influence on plasma albumin binding affinity of the derivatives. Our investigation proves that parallel with changes of lipophilic character and extent of plasma protein binding properties of Pa derivatives a consequent alteration occurs in their pharmacokinetic behavior without losing the pharmacodynamic effect. Based on our study a better understanding of the structural and biochemical behavior of different chemically modified flavonoid derivatives could be achieved making further design of in vivo experiments feasible.

Original languageEnglish
Pages (from-to)20-26
Number of pages7
JournalJournal of Photochemistry and Photobiology, B: Biology
Volume124
DOIs
Publication statusPublished - Jul 5 2013

Fingerprint

Hep G2 Cells
albumins
Albumins
flavone
tumors
cells
Taiwan
cultured cells
affinity
proteins
causes
rings
Hydroquinones
Ferns
Apigenin
protoapigenone
Tumor Cell Line
Flavonoids
Protein Binding
Serum Albumin

Keywords

  • Albumin binding
  • Anticancer effect
  • Cell viability
  • Flavonoids
  • Protoapigenone derivatives

ASJC Scopus subject areas

  • Radiation
  • Radiology Nuclear Medicine and imaging
  • Radiological and Ultrasound Technology
  • Biophysics

Cite this

Protoapigenone derivatives : Albumin binding properties and effects on HepG2 cells. / Poór, Miklós; Li, Yin; Kunsági-Máté, S.; Varga, Zsófia; Hunyadi, Attila; Dankó, Balázs; Chang, Fang Rong; Wu, Yang Chang; Kőszegi, T.

In: Journal of Photochemistry and Photobiology, B: Biology, Vol. 124, 05.07.2013, p. 20-26.

Research output: Contribution to journalArticle

Poór, Miklós ; Li, Yin ; Kunsági-Máté, S. ; Varga, Zsófia ; Hunyadi, Attila ; Dankó, Balázs ; Chang, Fang Rong ; Wu, Yang Chang ; Kőszegi, T. / Protoapigenone derivatives : Albumin binding properties and effects on HepG2 cells. In: Journal of Photochemistry and Photobiology, B: Biology. 2013 ; Vol. 124. pp. 20-26.
@article{c810e4ef951e41559bbd1a3592c2f585,
title = "Protoapigenone derivatives: Albumin binding properties and effects on HepG2 cells",
abstract = "Protoapigenone (Pa) is a flavone aglycone with a p-quinol structure in its B-ring. It was first discovered in Thelypteris torresiana, a native fern in Taiwan. Recent studies highlighted that protoapigenone and some of its derivatives show very potent anticancer activity against several types of tumors, using both in vitro and in vivo models. Despite the growing body of evidence on the selective anticancer potential of protoapigenone and its derivatives, no data are available on their pharmacokinetical properties. In our present research, albumin binding properties of Pa and seven different 1′-O-alkyl protoapigenone derivatives were analyzed as well as their biochemical effects on HepG2 tumor cell line in comparison with the flavone apigenin. Our results are in good accordance with the data of previous investigations of 1′-O-alkylated derivatives of protoapigenone (with the exception of isopropyl and allyl derivatives) showing similar or higher antitumor effects than Pa. Furthermore structural changes in Pa cause a very remarkable influence on plasma albumin binding affinity of the derivatives. Our investigation proves that parallel with changes of lipophilic character and extent of plasma protein binding properties of Pa derivatives a consequent alteration occurs in their pharmacokinetic behavior without losing the pharmacodynamic effect. Based on our study a better understanding of the structural and biochemical behavior of different chemically modified flavonoid derivatives could be achieved making further design of in vivo experiments feasible.",
keywords = "Albumin binding, Anticancer effect, Cell viability, Flavonoids, Protoapigenone derivatives",
author = "Mikl{\'o}s Po{\'o}r and Yin Li and S. Kuns{\'a}gi-M{\'a}t{\'e} and Zs{\'o}fia Varga and Attila Hunyadi and Bal{\'a}zs Dank{\'o} and Chang, {Fang Rong} and Wu, {Yang Chang} and T. Kőszegi",
year = "2013",
month = "7",
day = "5",
doi = "10.1016/j.jphotobiol.2013.04.002",
language = "English",
volume = "124",
pages = "20--26",
journal = "Journal of Photochemistry and Photobiology B: Biology",
issn = "1011-1344",
publisher = "Elsevier",

}

TY - JOUR

T1 - Protoapigenone derivatives

T2 - Albumin binding properties and effects on HepG2 cells

AU - Poór, Miklós

AU - Li, Yin

AU - Kunsági-Máté, S.

AU - Varga, Zsófia

AU - Hunyadi, Attila

AU - Dankó, Balázs

AU - Chang, Fang Rong

AU - Wu, Yang Chang

AU - Kőszegi, T.

PY - 2013/7/5

Y1 - 2013/7/5

N2 - Protoapigenone (Pa) is a flavone aglycone with a p-quinol structure in its B-ring. It was first discovered in Thelypteris torresiana, a native fern in Taiwan. Recent studies highlighted that protoapigenone and some of its derivatives show very potent anticancer activity against several types of tumors, using both in vitro and in vivo models. Despite the growing body of evidence on the selective anticancer potential of protoapigenone and its derivatives, no data are available on their pharmacokinetical properties. In our present research, albumin binding properties of Pa and seven different 1′-O-alkyl protoapigenone derivatives were analyzed as well as their biochemical effects on HepG2 tumor cell line in comparison with the flavone apigenin. Our results are in good accordance with the data of previous investigations of 1′-O-alkylated derivatives of protoapigenone (with the exception of isopropyl and allyl derivatives) showing similar or higher antitumor effects than Pa. Furthermore structural changes in Pa cause a very remarkable influence on plasma albumin binding affinity of the derivatives. Our investigation proves that parallel with changes of lipophilic character and extent of plasma protein binding properties of Pa derivatives a consequent alteration occurs in their pharmacokinetic behavior without losing the pharmacodynamic effect. Based on our study a better understanding of the structural and biochemical behavior of different chemically modified flavonoid derivatives could be achieved making further design of in vivo experiments feasible.

AB - Protoapigenone (Pa) is a flavone aglycone with a p-quinol structure in its B-ring. It was first discovered in Thelypteris torresiana, a native fern in Taiwan. Recent studies highlighted that protoapigenone and some of its derivatives show very potent anticancer activity against several types of tumors, using both in vitro and in vivo models. Despite the growing body of evidence on the selective anticancer potential of protoapigenone and its derivatives, no data are available on their pharmacokinetical properties. In our present research, albumin binding properties of Pa and seven different 1′-O-alkyl protoapigenone derivatives were analyzed as well as their biochemical effects on HepG2 tumor cell line in comparison with the flavone apigenin. Our results are in good accordance with the data of previous investigations of 1′-O-alkylated derivatives of protoapigenone (with the exception of isopropyl and allyl derivatives) showing similar or higher antitumor effects than Pa. Furthermore structural changes in Pa cause a very remarkable influence on plasma albumin binding affinity of the derivatives. Our investigation proves that parallel with changes of lipophilic character and extent of plasma protein binding properties of Pa derivatives a consequent alteration occurs in their pharmacokinetic behavior without losing the pharmacodynamic effect. Based on our study a better understanding of the structural and biochemical behavior of different chemically modified flavonoid derivatives could be achieved making further design of in vivo experiments feasible.

KW - Albumin binding

KW - Anticancer effect

KW - Cell viability

KW - Flavonoids

KW - Protoapigenone derivatives

UR - http://www.scopus.com/inward/record.url?scp=84877066071&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84877066071&partnerID=8YFLogxK

U2 - 10.1016/j.jphotobiol.2013.04.002

DO - 10.1016/j.jphotobiol.2013.04.002

M3 - Article

C2 - 23648796

AN - SCOPUS:84877066071

VL - 124

SP - 20

EP - 26

JO - Journal of Photochemistry and Photobiology B: Biology

JF - Journal of Photochemistry and Photobiology B: Biology

SN - 1011-1344

ER -