Diketo modification of curcumin affects its interaction with human serum albumin

Unravelling the molecular interaction of diselenodipropionic acid (DSePA) with human serum albumin (HSA)

“…These results suggest that DSePA quenches the fluorescence of HSA through static as well as dynamic quenching. 26,31 Therefore the fluorescence emission changes at 340 nm at different concentration of DSePA (5–50 μM) were fitted according to modified Stern-Volmer eqn (9). The intercept was obtained from the linear fit of the double logarithmic plot in the presence of varying concentration of DSePA.…”

“…Eventually, the favoured pose of the DSePA on the HSA as circulatory protein was evaluated by scoring method. 26…”

“…Eventually, the favoured pose of the DSePA on the HSA as circulatory protein was evaluated by scoring method. 26 3 Results and discussion The absorption spectra of varying concentration of HSA (5-120 mM) were followed in the absence and presence (20 mM) of DSePA (Fig. 1) to estimate exact increase in absorbance value upon addition of DSePA.…”

“…[44][45][46] For simulating the binding of HSA with DSePA by molecular docking, the optimized or building up chemical structures of DSePA were accustomed and the LeadIT software was employed, which considers the hybrid model of enthalpy and entropy mode of molecular interactions. 26 The most preferred binding site was determined on the basis of scoring and the standard free energy change (DG1) of DSePA on HSA protein was calculated. Here, we have observed that the most stable site for binding is in the domain IIA of HSA for DSePA (Fig.…”

“…2,24 HSA is an important extracellular carrier protein in humans; it possesses a unique capability to bind non-covalently (such as van der Waals forces, hydrogen bonding and ionic interactions) and transport a wide variety of endogenous and exogenous nutrients as well as drugs to the cells. [25][26][27][28][29] This monomeric globular protein is composed of three homologous domains, domain I (amino acid residues 1-195), domain II (196-383; site I) and domain III (384-585; site II), respectively. Each domain part has two sub-domains, viz.…”