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�105 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 DG value (−32.93 kJ mol−1) for the complex at 298 K. Additionally, the effects of Ca2þ, Mg2þ, and Zn2þ on binding properties were evaluated by fluorescence spectroscopy. The binding constant of the complex was recorded as 6.76�103 in the presence of Zn2þ and 5.93�105 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.