Abstract
The interaction between the anti-HIV drug Elvitegravir (EVG) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy and UV-visible absorption spectra. The mechanism for quenching the fluorescence of BSA by EVG is discussed. It was found that EVG can quench the intrinsic fluorescence of BSA through a static quenching procedure. The quenching type, association constant, and number of binding sites were investigated. The binding constant of EVG with BSA was calculated at different temperatures based on fluorescence quenching results. The thermodynamic parameters
Δ
H
θ
,
Δ
G
θ
, and
Δ
S
θ
were determined. The positive
Δ
S
θ
and negative
Δ
H
θ
and
Δ
G
θ
values showed that a spontaneous interaction may involve both roles of hydrophobic interaction and hydrogen bonding. The interaction of BSA with EVG was also confirmed by UV absorption spectra. The average distance,
r
, between donor (BSA) and acceptor (EVG) was obtained according to Förster’s theory of nonradiation energy transfer. Synchronous fluorescence and three-dimensional fluorescence spectra were used to investigate the conformational change of BSA molecules that occur upon addition of EVG and showed, upon binding, a possibility of increasing hydrophobicity around tryptophan residues of BSA.