Fluorescence investigation of the interaction of 2-(4-fluorophenyl)-1-phenyl-1H-phenanthro [9,10-d] imidazole with bovine serum albumin

Investigation of the interaction of anthraquinones of Cassia occidentalis seeds with bovine serum albumin by molecular docking and spectroscopic analysis: Correlation to their in vitro cytotoxic potential

“…BSA showed characteristic emission peak at 343 nm upon excitation at 280 nm, which is mainly due to the tryptophan residue present in the hydrophobic core of the protein (Zhang et al, 2013). The gradual decrease in fluorescence intensity with increasing concentration of test compounds is generally analyzed by stern volmer equation and used to calculate the different binding characteristics including K q , K a , K sv and n. In the present study, the intrinsic fluorescence quenching of BSA by all the five AQs, suggests the higher value of K q than the maximum value of scattering collision quenching constant/limiting rate diffusion constant (2.0 × 10 10 L mol -1 s -1 ), which indicates that the probable quenching mechanism of BSA-AQ binding are static and initiated by ground state complex formation (Jayabharathi et al, 2012). Furthermore, high values of dynamic quenching constant (K sv ) (Sharma et al, 2013) Since, liver is the primary target organ for toxicity of CO seeds as well as its toxic components (anthraquinones) (Panigrahi et al, 2014b(Panigrahi et al, , 2015Bironaite and Ollinger, 1997); in the present study the cytotoxicity of anthraquinones present in CO seeds were examined both in rat primary hepatocytes and human cell hepatoma cells (HepG2).…”

Mechanism of Dimercaptosuccinic Acid Coated Superparamagnetic Iron Oxide Nanoparticles with Human Serum Albumin

“…The spectrum is measured by the excitation and emission monochromators through the simultaneous scanning while maintaining a constant wavelength interval between them. When the wavelength intervals ( λ) are kept at 15 or 60 nm, the synchronous fluorescence gives the characteristic information of Tyr residues or Trp residues, respectively [29,30]. The synchronous fluorescence spectra of HSA with different concentrations of SPION in Figure 3B (the inner filter effect was corrected) showed that the emission peaks have a blueshift, which indicated that SPION has effect on the microenvironment of the Tyr residues in HSA that the polarity around Tyr residues changed and the binding placed the Tyr residues in a less hydrophilic environment.…”

Binding interactions of niclosamide with serum proteins

“…where F 0 and F are the fluorescence intensities of the proteins before and after the addition of the quencher; K q is the quenching constant; K SV is the SterneVolmer quenching constant; [Q] is the concentration of the quencher; and s 0 is the average biomolecular fluorescence lifetime, which is considered to be 10 À8 seconds [25,26]. The SterneVolmer plots at different temperatures are given in Fig.…”