Interactions of cannabinoids with bovine serum albumin

There is no shift of emission maximum (F₄₇₀nm) of bovine serum albumin (BSA)-l-anilino-8-naphthatene sulphonic acid (ANS) complex in the pesence of delta-9-tetrahydrocannabinol (delta-9-THC) alone and cannabidiol (CBD) or cannabinol (CBN) in the presence and absence of delta-9-THC. Delta-9-THC (1.66–13.33 μM) and CBD at higher concentrations (13.33–20.0 μM) produce a concentration-dependent significant quenching of fluorescence of BSA-ANS complex, but CBN (l.66–20.0 μM) as well as CBD at lower concentrations (1.66–6.66 μM) fails to produce any significant change in Iluorescence intensity under similar conditions. Furthermore, neither CBD nor CBN is able to affect the delta-9-THC-induced quenching of fluorescence intensity of BSA-ANS complex. These results indicate that the binding of cannabinoids to the ANS binding sites of BSA molecule are in the order detta-9-THC > CBr3 > CBN, and CBD or CBN does not have any influence on the binding of delta-9-THC to BSA molecules under these conditions.