Abstract
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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
