Enhanced Transport of Nandrolone Decanoate Drug by Human Serum Albumin in Presence of [BMIM]PF6 and [BMIM]BF4.

ABSTRACT

The interaction of nandrolone decanoate drug dissolved in (2%) [BMIM]BF4 or [BMIM]PF6 with human serum albumin (HSA) at different temperatures in the range of 285-310 K was examined by fluorescence quenching. Stern-Volmer equation and its modified form were used to determine the interaction parameters K and n. The results revealed that binding affinities of HSA for nandrolone decanoate drug in 2% [BMIM]BF4 or [BMIM]PF6 are in the order of 105 M-1 and the number of bound drug molecules per HSA macromolecule are approximated to 1 at all temperatures studied. The thermodynamic parameters free energy change (∆Go), enthalpy change (∆Ho) and entropy change (∆So) for HSA-nandrolone decanoate/ionic liquid were calculated according to van't Hoff equation. Data analysis indicated that both electrostatic interactions and hydrophobic ineractions played important roles in the interaction of nandrolone decanoate drug with HSA.