Ferutinin stability in human plasma and interaction with human serum albumin

Ferutinin is a potent phytoestrogen extracted from plants of the genus Ferula. The biological activity of this sesquiterpene is associated with the esterification of p‐hydroxybenzoic acid with the daucane alcohol, jaeschkeanadiol. A HPLC method was developed to investigate the stability of ferutinin in acidic and basic solutions (pH 1.5 and 9.0, respectively), in buffer (pH 7.4) as well as in serial dilutions of albumin and in human plasma. The degradation of ferutinin was relatively slow at physiological pH 7.4 compared with low or high pH. Ferutinin was fully stable in human plasma as well as in albumin solution and the stability increased with albumin concentration. The binding of ferutinin to albumin was investigated by fluorescence spectroscopy. Ferutinin decreased the fluorescence of HSA and that of the only tryptophan residue located in domain IIA. As a result of the interaction between ferutinin and albumin, the binding of bilirubin decreased. The stability of ferutinin in plasma is attributable to ferutinin–albumin binding. Copyright © 2007 John Wiley & Sons, Ltd.

[1]  Feng Yang,et al.  Effect of human serum albumin on drug metabolism: structural evidence of esterase activity of human serum albumin. , 2007, Journal of structural biology.

[2]  C. Haddad,et al.  Effect of cucurbitacins on bilirubin-albumin binding in human plasma. , 2007, Life sciences.

[3]  A. Bahsas,et al.  Ferutinin stimulates nitric oxide synthase activity in median eminence of the rat. , 2006, Journal of ethnopharmacology.

[4]  E. Duysen,et al.  Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma. , 2005, Biochemical pharmacology.

[5]  N. Fabre,et al.  Daucane sesquiterpenes from Ferula hermonis. , 2005, Journal of natural products.

[6]  B. Fiebich,et al.  Calcium ionophoretic and apoptotic effects of ferutinin in the human Jurkat T-cell line. , 2004, Biochemical pharmacology.

[7]  S. Milligan,et al.  Structure--activity relationships of the estrogenic sesquiterpene ester ferutinin. Modification of the terpenoid core. , 2004, Journal of natural products.

[8]  L. Trynda-Lemiesz.  Paclitaxel-HSA interaction. Binding sites on HSA molecule. , 2004, Bioorganic & medicinal chemistry.

[9]  N. Yamaotsu,et al.  Esterase-Like Activity of Serum Albumin: Characterization of Its Structural Chemistry Using p-Nitrophenyl Esters as Substrates , 2004, Pharmaceutical Research.

[10]  R. H. Khan,et al.  Intermediate formation at lower urea concentration in 'B' isomer of human serum albumin: a case study using domain specific ligands. , 2004, Biochemical and biophysical research communications.

[11]  M. Ramanathan,et al.  A Rapid Spectrofluorimetric Technique for Determining Drug-Serum Protein Binding Suitable for High-Throughput Screening , 2000, Pharmaceutical Research.

[12]  G. Cravotto,et al.  Daucane phytoestrogens: a structure-activity study. , 2002, Journal of natural products.

[13]  J. M. Clancy,et al.  Isosorbide-based aspirin prodrugs. II. Hydrolysis kinetics of isosorbide diaspirinate. , 2002, European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences.

[14]  S. Kato,et al.  Terpenoids Found in the Umbelliferae Family Act as Agonists/Antagonists for ERα and ERβ: Differential Transcription Activity between Ferutinine-Liganded ERα and ERβ , 2002 .

[15]  I. Khan,et al.  Separation and quantification of the major daucane esters of Ferula hermonis by HPLC. , 2001, Planta medica.

[16]  E. Abourashed,et al.  Daucane sesquiterpenes from Ferula hermonis. , 2001, Journal of natural products.

[17]  J. Bessière,et al.  Daucane aryl esters composition from the Lebanese Ferula hermonis Boiss. (zallooh root) , 2001 .

[18]  Saad Tayyab,et al.  On the modulation of photoinduced fluorescence enhancement and conformational stability of albumin-bound bilirubin: effect of epsilon-NH(2) groups blocking and chloroform binding. , 2000, Biochimica et biophysica acta.

[19]  P. Merzlyak,et al.  Ionophoretic properties of ferutinin. , 1997, Cell calcium.

[20]  D. Watts,et al.  Kinetics of the degradation of methyl, ethyl and n-propyl 4-hydroxybenzoate esters in aqueous solution , 1984 .

[21]  R. Wennberg,et al.  The effect of paraben preservatives on albumin binding of bilirubin. , 1976, The Journal of pediatrics.

[22]  R. F. Chen,et al.  Fluorescence stopped-flow study of relaxation processes in the binding of bilirubin to serum albumins. , 1974, Archives of biochemistry and biophysics.

[23]  R. Mayer,et al.  Binding study of p-hydroxybenzoic acid esters to bovine serum albumin by fluorescent probe technique. , 1971, Journal of pharmaceutical sciences.