Department of Chemistry, Sardar Vallabhbhai National Institute of Technology, Surat 395007, Gujarat, India.
Department of Chemistry, Sardar Vallabhbhai National Institute of Technology, Surat 395007, Gujarat, India.
Methods. 2022 Oct;206:69-76. doi: 10.1016/j.ymeth.2022.08.014. Epub 2022 Aug 29.
The detection of albumin proteins with high accuracy by facile analytical approaches is important for the diagnosis of various diseases. This manuscript introduced an easy-to-prepare Schiff base L by condensing vitamin B cofactor pyridoxal 5'-phosphate (PLP) with 2-aminothiophenol for the fluorescence turn-on sensing of bovine serum albumin (BSA) and ovalbumin (OVA). The weakly emissive L showed a significant fluorescence enhancement at 485 and 490 nm in the presence of OVA and BSA with an estimated sensitivity limit of 1.7 µM and 0.3 µM, respectively. The formation of protein-ligand complex restricted the free intramolecular rotation of L is expected to show the selective fluorescence enhancement. The molecular docking and molecular dynamics simulations were performed to examine the binding affinity and modes between BSA/OVA and L. The practical utility of L as a fluorescent turn-on sensor was validated by quantifying BSA and OVA in various real biological samples of milk, serum, egg white and urine with good recovery percentages.
通过简便的分析方法准确检测白蛋白蛋白对于各种疾病的诊断非常重要。本文介绍了一种易于制备的席夫碱 L，它是通过将维生素 B 辅因子吡哆醛 5'-磷酸（PLP）与 2-氨基噻吩缩合而成，用于牛血清白蛋白（BSA）和卵清蛋白（OVA）的荧光开启传感。弱发光的 L 在存在 OVA 和 BSA 时在 485 和 490nm 处显示出显著的荧光增强，其估计的灵敏度极限分别为 1.7µM 和 0.3µM。蛋白质-配体复合物的形成限制了 L 的自由分子内旋转，预计会显示出选择性的荧光增强。进行了分子对接和分子动力学模拟，以检查 BSA/OVA 和 L 之间的结合亲和力和模式。通过在牛奶、血清、蛋清和尿液等各种实际生物样本中定量测定 BSA 和 OVA，验证了 L 作为荧光开启传感器的实际应用，具有良好的回收率。
