Synthesis, characterization, and BSA binding studies of newfangled 2-phenylacetohydrazide derivatives

Five 2-phenylacetohydrazide derivatives (BPAH = <i>N</i>'-benzylidene-2-phenylacetohydrazide, HBPAH = <i>N</i>'-(2-hydroxybenzylidene)-2-phenylacetohydrazide), PPAH = 2-phenyl-<i>N'</i>-3-phenylallylideneacetohydrazide, FMPAH = <i>N'</i>-(furan-2-ylmethylene)-2-phenylaceto hydrazide and EPAH = <i>N'</i>-ethylidene-2-phenylacetohydrazide were synthesized by the condensation of 2-phenylacetohydrazide with the corresponding aldehyde. The synthesized compounds were characterized by FTIR, 1D, and 2D NMR spectroscopy. The structure of the BPAH and PPAH were analyzed by single crystal X-ray diffraction analysis and in both crystallized compounds, the molecules adopted <i>trans</i> geometry around the -C[bond, double bond]N- (imine) functional group. To explore the pharmacological significance of these compounds, the binding ability of these compounds with Bovine Serum Albumin (BSA) was investigated using fluorescence spectroscopy. BPAH and PPAH showed the highest binding ability while EPAH, HBPAH, and FMPAH had lower binding ability to BSA molecules. Thermodynamic parameters <i>ΔG</i>, <i>ΔH°,</i> and <i>ΔS°</i> demonstrated that interactions of BSA with compounds BPAH, EPAH, FMAH, and HBPAH were exothermic while for PPAH it was endothermic. The negative enthalpy and entropy of the compounds BPAH, EPAH, FMAH, and HBPAH indicated that van der Waals<i>'</i> forces and hydrogen bonding played a major role in stabilizing the BSA binding with the molecules. Hydrophobic interactions were predominant in the binding of PPAH with BSA tends to interact with two sets of BSA binding sites with an increase in temperature.