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.