Effects of urea, metal ions and surfactants on the binding of baicalein with bovine serum albumin.

ABSTRACT: The interaction of baicalein with bovine serum albumin (BSA) was investigated with the help of spectroscopic and molecular docking studies. The binding affinity of baicalein towards BSA was estimated to be in order of 10⁵ M^-1 from fluorescence quenching studies. Negative ΔH° (-5.66±0.14 kJ/mol) and positive (ΔS°) (+79.96±0.65 J/mol K) indicate the presence of electrostatic interactions along with the hydrophobic forces that result in a positive ΔS°. The hydrophobic association of baicalein with BSA diminishes in the presence of sodium dodecyl sulfate (SDS) due to probable hydrophobic association of baicalein with SDS, resulting in a negative ΔS° (-40.65±0.87 J/mol K). Matrix-assisted laser desorption ionization/time of flight (MALDI--TOF) e

SUBMITTER: Roy AS 

PROVIDER: S-EPMC5762607 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature