Combined spectroscopy methods and molecular simulations for the binding properties of trametinib to human serum albumin.

ABSTRACT: Trametinib is a novel anticancer drug for treating metastatic cutaneous melanoma. The present study probed into the binding of trametinib to human serum albumin (HSA) through spectroscopy methods and molecular simulations. Trametinib could quench the fluorescence of HSA through static quenching which could be probed via fluorescence spectroscopy and time-resolved fluorescence. Thermodynamic parameters and docking results indicated that hydrogen bonds and van der Waals forces play crucial roles in this binding process, which exerts almost no effect on the HSA conformation under synchronous fluorescence, three-dimensional fluorescence, circular dichroism spectra, and molecular dynamics simulations. Site marker displacement experiments and molecular docking reveal that trametinib prima

SUBMITTER: Suo Z 

PROVIDER: S-EPMC9077761 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature