Interaction analysis of a new NHC precursor and its Ag-NHC complex with bovine serum albumin by spectrophotometric and molecular docking methods

Abstract

Potential bioactive molecules must reach the target tissue safely and serum albumin, which is a well-known major component in human blood, is an efficient transporter. Therefore, the interactions of possible bioactive species with serum albumin must be determined. In the current study, an N-heterocyclic carbene precursor and its silver complex were synthesized, characterized, and analyzed for interactions with bovine serum albumin. Stern-Volmer constant was recorded as 4.50 x 10(5) for Ag-NHC with a 1.255 binding number at 298 K. Also, the molecules have spontaneously interacted with bovine serum albumin with a negative Delta G value (-32.93 kJ mol(-1)) for the complex at 298 K. Additionally, the effects of Ca2+, Mg2+, and Zn2+ on binding properties were evaluated by fluorescence spectroscopy. The binding constant of the complex was recorded as 6.76 x 10(3) in the presence of Zn2+ and 5.93 x 10(5) without the metals. The molecules were optimized by DFT-based calculations and the details of the bindings were investigated by molecular docking methods. Ag-NHC has interacted with the IIA subdomain region of bovine serum albumin with -8.46 kcal/mol. [GRAPHICS] .