Essential oil (EO) from Eucalyptus polybrachtea is used as complementary and
traditional medicine worldwide. The present study aimed at compositional profiling of EO and molecular docking of EO's bioactive compound
1,8 cineole against fungal
enzymes involved in the
riboflavin synthesis pathway, namely
riboflavin synthase (RS),
riboflavin biosynthesis protein RibD domain-containing
protein (RibD), and
3,4-dihydroxy-2-butanone 4-phosphate synthase (
DBPS) as apposite sites for
drug designing against
aspergillosis and
mucormycosis, and in vitro confirmation. The compositional profile of EO was completed by GC-FID analysis. For molecular docking, the Patchdock tool was used. The
ligand-
enzyme 3-D interactions were examined, and ADMET properties (absorption, distribution, metabolism, excretion, and toxicity) were calculated. GC-FID discovered the occurrence of
1,8 cineole as a major component in EO, which was subsequently used for docking analysis. The docking analysis revealed that
1,8 cineole actively bound to RS, RibD, and
DBPS fungal
enzymes. The results of the docking studies demonstrated that the
ligand 1,8 cineole exhibited H-bond and hydrophobic interactions with RS, RibD, and
DBPS fungal
enzymes.
1,8 cineole obeyed Lpinsky's rule and exhibited adequate bioactivity. Wet-lab authentication was achieved by using three fungal strains: Aspergillus niger, Aspergillus oryzae, and Mucor sp. Wet lab results indicated that EO was able to inhibit fungal growth.