Abstract
The interactions of human CYP3A4 with three selected isomer flavonoids, such as astilbin, isoastilbin and neoastilbin, are clarified using spectral analysis, molecular docking and molecular dynamics simulation. During binding with the three flavonoids, the intrinsic fluorescence of CYP3A4 is statically quenched in static mode with non-radiative energy conversion. The fluorescence and UV/Vis data reveal that the three flavonoids have moderate and stronger binding affinity with CYP3A4 due to the order of Ka1 and Ka2 values ranged from 104 to 105 L·mol-1 . In the meantime, astilbin has the highest affinity with CYP3A4, then isoastilbin and neoastilbin at the three experimental temperatures. Multispectral analysis confirms that the binding of the three flavonoids results in clear changes in the secondary structure of CYP3A4. It can be found from fluorescence, UV/Vis and molecular docking that these three flavonoids strongly bind to CYP3A4 by the means of hydrogen bond and van der Waals forces. The key amino acids around the binding site are also elucidated. Furthermore, the stabilities of the three-CYP3A4 complexes are evaluated by molecular dynamics simulation.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
More From: Luminescence : the journal of biological and chemical luminescence
Disclaimer: 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.