The interaction between the plasma protein bovine serum
albumin
(BSA) and the drug ibuprofen (IBU) has been investigated at three
different pH values (7.4, 6.5, and 8.0) in the presence of oligosaccharides
and surfactants. The interaction analysis of BSA with oligosaccharides
and surfactants has also been studied in the absence of the drug ibuprofen.
The results obtained give convenient and efficient access to understand
the mechanism of binding of ibuprofen to BSA, and the major forces
involved are found to be hydrophobic forces, hydrogen bonding and
ionic interactions. In addition to that, the formation of inclusion
complexes of ibuprofen with oligosaccharides (β-CD and 2-HP-β-CD)
has been observed, which has depicted that due to the hydrophobic
nature of ibuprofen, it becomes more soluble in the presence of oligosaccharides,
but due to the larger size of the inclusion complexes, these could
not be able to access the hydrophobic pocket of BSA where tryptophan-212
(Trp-212) resides. The binding interaction between BSA and ibuprofen
is observed in the presence of surfactants (SDS and CTAB), which partially
unfold the protein. Non-radiative fluorescence resonance energy transfer
(FRET) from Trp and Tyr residues of BSA in the presence of an anionic
surfactant SDS to ibuprofen has depicted that there is a possibility
of drug binding even in the partially unfolded state of BSA protein.
Furthermore, the distance between the protein and the drug has been
calculated from the FRET efficiency, which gives a comprehensive overview
of ibuprofen binding to BSA even in its partially denatured state.
The hydrophobic drug binding to the partially unfolded serum albumin
protein (BSA) supports the “necklace and bead structures”
model and opens up a new direction of drug loading and delivery system,
which will have critical therapeutic applications in the efficient
delivery of pharmacologically prominent drugs.