Effects of black cumin-based antimalarial drug loaded with nano-emulsion of bovine and human serum albumins by spectroscopic and molecular docking studies.

The growing understanding of nanoemulsion biomedical applications necessitates a basic understanding of protein-drug-loaded nanoemulsion interaction. In our present study, we investigated the binding interactions of Mefloquine (MEF)-loaded black cumin seed oil (Thymoquinone) nanoemulsion of different concentrations towards human and bovine serum albumin (HSA&BSA).Fluorescenceemission,three-dimensionalspectra,UV-visible spectroscopy, and FTIR-spectroscopy, techniques were used together with molecular docking studies to identify the binding effects. The ground state complex formation between Mefloquine-loaded black cumin seed oil nanoemulsion and protein fluorophores was confirmed by a decrease in fluorescence intensity and disputed hyper-chronicity found in the UV-visible spectra of albumins. According to three-dimensional fluorescence spectral analysis, the addition of MEF in thymoquinone impacted the microenvironment around aromatic amino acid (tryptophan and tyrosine) residues in HSA. The quenching mechanism is determined to be static contact by stern-volmer analysis, resulting in the formation of a stable bioconjugate. Significant modifications in the amide FTIR frequencies at around 1600 cm correlate to variations in the secondary alpha-helical structures of biomolecules at the MEF-loaded nanoemulsion interface. Molecular dynamic studies have shown the binding affinity scores of the proteins BSA and HSA with the drug, MEF-loaded black cumin seed oil nanoemulsion. The determined thermodynamic parameters were found to agree with molecular docking data, indicating that vander-waals and hydrogen bonding forces were important in the interaction process. MEF prefers a highly polar binding site at the exterior area of domains in HSA than BSA, as shown in the molecular model, and the hydrogen bonds are highlighted. From our results, we have observed that drug delivery has a detrimental effect on protein frame confirmation by altering its physiological function.