Study on the interaction of food colourant quinoline yellow with bovine serum albumin by spectroscopic techniques

Inhibition of chrysin on xanthine oxidase activity and its inhibition mechanism

“…As shown in Fig. 5, the CD spectrum of XO exhibited two negative double humped peaks in the ultraviolet region at 208 and 222 nm, which were the characteristic peaks caused by the transition of → and n → * of ␣-helix structure [40]. With the molar ratios of chrysin to XO increased from 0:1 to 1:1 and 2:1, the CD signal of XO was obviously enhanced.…”

Inhibitory effect of synthetic aromatic heterocycle thiosemicarbazone derivatives on mushroom tyrosinase: Insights from fluorescence, 1 H NMR titration and molecular docking studies

“…For the static quenching interaction, if it is assumed that there are similar and independent sites in the biomolecule, the apparent binding constant (K a ) and the number of binding sites (n) can be calculated by the following equation (Shahabadi, Maghsudi, & Rouhani, 2012):…”

Kinetic studies of bovine serum albumin interaction with PG and TBHQ using surface plasmon resonance

“…Because of having multiple lipophilic binding sites located in subdomains IIA and IIIA, serum albumins are capable of transporting and distributing of endogenous and exogenous compounds like various ligands, vitamins, hormones, drugs, nutrients, food additives and other physiological substances [2][3][4][5][6][7]. With increasing the amount of binding affinity between these proteins and compounds, free concentration and the physiological activity of various materials such as drugs decreased in blood plasma.…”