| Lawsonia inermis L. (Henna) has been widely used in cosmetic, medicine and pharmacy industries. Henna is one
of the ancient used plants and it can be absorbed into the blood and interact with plasma serum albumin. In this
article, we investigated the interaction between henna and bovine serum albumin (BSA) through several spectroscopic techniques, which accompanied with molecular docking approach. According to the results, fluorescence
intensity of BSA were decreased upon addition of different concentrations of henna and variation of the intensity
illustrates the interaction between henna and BSA. Stern-Volmer quenching analysis along with bimolecular
quenching rate results suggested that henna quenched the intensity of BSA through hybrid quenching mechanism, which was con firmed via UV–Vis measurement. As the temperature increase, values of binding constant
increased from 5.17 × 102 to 6.17× 102 (M −1) demonstrating that the stability of henna –BSA complex increased
with temperature rising. Thermodynamic investigations revealed that the henna molecule bind to BSA via hydrophobic bonds spontaneously. Furthermore, the molecular docking analysis demonstrated that henna has high affinity to bind a cavity in Site II (Domain III, subdomain IIIA) on BSA with binding energy score - 11.37 kcal/mol.
Finally, it should be stated that distribution of the henna in the blood circulatory system can be done via BSA,
which would accompany us to understand the different medicinal aspects of this natural product especially in
drug delivery. |