Characterization of the binding of nevadensin to bovine serum albumin by optical spectroscopic technique

Binding of nevadensin to bovine serum albumin (BSA) has been studied in detail at 298 and 310 K using spectrophotometric technique. The intrinsic fluorescence of BSA was strongly quenched by the addition of nevadensin and spectroscopic observations are mainly rationalized in terms of a static quenching process at lower concentration of nevadensin (C-drug/C-BSA < 1) and a combined quenching process at higher concentration of nevadensin (C-drug/C-BSA > 1). The binding parameters for the reaction at a pH above (7.40) or below (3.40) the isoelectric point have been calculated according to the double logarithm regression curve. The thermodynamic parameters Delta H-0, Delta G(0), Delta S-0 at different temperatures and binding mechanism of nevadensin to BSA at pH 7.40 and 3.40 were evaluated. The binding ability of nevadensin to BSA at pH 7.40 was stronger than that at pH 3.40. Steady fluorescence, synchronous fluorescence and circular dichroism (CD) were applied to investigate protein conformation. A value of 2.15 nm for the average distance r between nevadensin (acceptor) and tryptophan residues (Trp) of BSA (donor) was derived from the fluorescence resonance energy transfer. Moreover, influence of pH on the interaction nevadensin with BSA was investigated. (C) 2008 Elsevier B.V. All rights reserved.