A novel hydrazone, (E)-Ethyl-4-(2-(furan-2-ylmethylene)hydrazinyl)benzoate (EFHB), has been synthesized and characterized by FT-IR, NMR and Mass spectroscopy, and X-ray diffraction; compound crystallized as translucent light yellow thin plates. EFHB was studied for their binding to human serum albumin (HSA) using the fluorescence quench titration method. Molecular docking was also performed to get a more detailed insight into their interaction with HSA at the binding site. Addition of this hydrazone to HSA produced significant fluorescence quenching and splitting of emission spectra of HSA through static quenching mechanism with binding constants of about 10⁴ M⁻¹ at 292.15, 298.15, 304.15 and 310.15 K. According to the synchronous fluorescence, tryptophan and tyrosine residues of the protein are most perturbed by the binding process. Thermodynamic parameters ΔG, ΔH, and ΔS were got and the main sort of acting force between EFHB and HSA was studied. Results of molecular docking have shown that EFHB binds to subdomain IIA of HSA mainly by hydrophobic interaction, energy binding are in good agreement with those obtained by fluorescence study (ΔG_the = −7.32 ± 0.09 kcal mol⁻¹ and ΔG_exp = −6.76 ± 0.03 kcal mol⁻¹).

合成了一种新型的（E）-4-（2-（呋喃-2-基亚甲基）肼基）苯甲酸乙酯（EFHB），并通过FT-IR，NMR，质谱和X射线衍射进行了表征。化合物结晶为半透明的浅黄色薄板。使用荧光猝灭滴定法研究了EFHB与人血清白蛋白（HSA）的结合。还进行了分子对接，以更详细地了解它们与结合位点与HSA的相互作用。将此添加到HSA中可通过静态猝灭机理产生显着的荧光猝灭和HSA发射光谱的分裂，其结合常数约为10 ⁴ M ^-1在292.15、298.15、304.15和310.15 K处。根据同步荧光，蛋白质的色氨酸和酪氨酸残基受结合过程的干扰最大。热力学参数Δ ģ，Δ ħ，和Δ小号分别得到和EFHB和HSA之间作用力的主要种类进行了研究。分子对接的结果表明，EFHB主要通过疏水相互作用与HSA的亚结构域IIA结合，能量结合与通过荧光研究获得的能量结合良好（ΔG _the  = -7.32±0.09 kcal mol ^-1和ΔG _exp  =- 6.76±0.03kcal mol ^-1）。