Abstract:

The interaction of ergosterol with bovine serum albumin (BSA) was investigated by fluorescence spectroscopy
and molecular docking. The fluorescence spectral results showed that BSA fluorescence was quenched regularly with the addition
of ergosterol; the quenching mechanism may be a static fluorescence quenching process; the thermodynamic parameters calculated
by Van’t Hoff equation indicated the major role of hydrophobic interaction in the binding process. Consistent results were obtained
from the molecular docking. Hydrophobic interaction was the major interaction, and the binding site of ergosterol on BSA was in
a hydrophobic binding pocket, and the binding was a spontaneous process. In addition, the detailed binding mode of ergosterol and
the conformation of the surrounding residues were shown in docking results.

Key words: ergosterol, bovine serum albumin (BSA), fluorescence quenching, molecular docking, binding site