两种吡咯基化合物,1H-吡咯并[3,2-b]吡啶-3-甲酸(L1)和1H-吡咯并[3,2-c]吡啶-4-甲酸(L2),在磷酸盐缓冲溶液(pH=7)中通过UV-Vis和荧光光谱法检测牛血清白蛋白(BSA)。在存在L1和L2的情况下,BSA在340nm处的荧光发射被猝灭,并且伴随地在420nm(L1)/450nm(L2)处出现红移发射带。荧光光谱变化表明BSA和L1/L2之间的蛋白质-配体复合物形成。进行等温滴定量热法(ITC)实验以确定BSA与L1/L2之间的结合能力。发现L1的结合常数分别为4.45±0.22×104M-1,L2的结合常数分别为2.29±0.11×104M-1。热力学参数由ITC测量值计算得出(即ΔrH=-40±2kcal/mol,ΔrG=-4.57±0.22千卡/摩尔和-TΔrS=35.4±1.77千卡/摩尔),这表明L1/L2与BSA之间的蛋白质-配体复合物的形成主要是由于静电相互作用。通过进行分子对接研究了蛋白质-配体相互作用。Further,我们对革兰氏阳性和革兰氏阴性菌株进行了L1和L2的抗菌试验,以解决抗菌和多重耐药细菌同时出现所带来的困难.大肠杆菌和金黄色葡萄球菌被L1和L2显著抑制。L1表现为13、12和15毫米,而L2对金黄色葡萄球菌具有2、3和5mm的抑制作用,美国化脓性细菌和大肠杆菌,分别。用细菌DNA促旋酶进行L1和L2的计算机分子对接以建立分子间相互作用。最后,配体L1和L2的体外细胞毒性活性已使用果蝇进行。
Two pyrrolo-based compounds, 1H-pyrrolo[3,2-b]pyridine-3-carboxylic acid (L1) and 1H-pyrrolo[3,2-c]pyridine-4-carboxylic acid (L2), were employed for the detection of bovine serum albumin (
BSA) by UV-Vis and fluorescence spectroscopic methods in phosphate buffer solution (pH = 7). In the presence of L1 and L2, the fluorescence emission of
BSA at 340 nm was quenched and concomitantly a red-shifted emission band appeared at 420 nm (L1)/450 nm (L2). The fluorescence spectral changes indicate the protein-ligand complex formation between
BSA and L1/L2. An isothermal titration calorimetry (ITC) experiment was conducted to determine the binding ability between
BSA and L1/L2. The binding constants are found to be 4.45 ± 0.22 × 104 M-1 for L1 and 2.29 ± 0.11 × 104 M-1 for L2, respectively. The thermodynamic parameters were calculated from ITC measurements (i.e. ∆rH = -40 ± 2 kcal/mol, ∆rG = -4.57 ± 0.22 kcal/mol and -T∆rS = 35.4 ± 1.77 kcal/mol), which indicated that the protein-ligand complex formation between L1/L2 with
BSA is mainly due to the electrostatic interactions. The protein-ligand interactions were studied by performing molecular docking. Further, the antibacterial assay of L1 and L2 was conducted against gram-positive and gram-negative bacterial strains in an effort to address the difficulties caused by the co-occurrence of antimicrobial and multidrug-resistant bacteria. E. coli and S. aureus were significantly inhibited by L1 and L2. The L1 exhibits 13, 12 and 15 mm, whereas L2 exhibits a 2, 3 and 5 mm zone of inhibition against S. aureus, S. pyogenes and E. coli, respectively. In silico molecular docking of L1 and L2 was performed with bacterial DNA gyrase to establish the intermolecular interactions. Finally, the in vitro cytotoxicity activities of the ligands L1 and L2 have been carried out using drosophila.