Department of Chemistry, Jadavpur University, Kolkata 700032, India.
Department of Chemistry, Jadavpur University, Kolkata 700032, India.
Spectrochim Acta A Mol Biomol Spectrosc. 2018 Apr 15;195:7-15. doi: 10.1016/j.saa.2018.01.029. Epub 2018 Jan 12.
Interest in synthesizing and characterizing (IR, NMR and HRMS spectroscopic methods) a pyrimidine based Schiff-base ligand, 2-(2-(Anthracen-9-ylmethylene) hydrazinyl)-4,6-dimethyl pyrimidine (ANHP) has been developed for its application to ascertain the conformational change of protein and sensitivity towards fluorescence resonance energy transfer (FRET) process. Location of ANHP in bovine serum albumin (BSA) and human serum albumin (HSA) proteins environment has been determined using different spectroscopic techniques. Weakly fluorescent ANHP have shown greater protein induced fluorescence enhancement (PIFE) in case of HSA than BSA, though in both cases energy transfer efficiency are almost same but difference in binding constant values encourages us to find the location of ANHP within the complex protein environment. From the FRET parameter and α-helicity change, it has been found that ANHP bound with Trp-214 of HSA and surface Trp-134 of BSA. Conformational changes of proteins have been observed more for HSA than BSA in presence of ANHP, which has confirmed the location of ANHP in both the protein environments. Coupled with experimental studies, molecular docking analysis has also been done to explain the locations and distance dependent FRET process of ANHP in both proteins.
人们对合成和表征（IR、NMR 和 HRMS 光谱方法）嘧啶类席夫碱配体 2-(2-(蒽-9-亚甲基)腙基)-4,6-二甲基嘧啶（ANHP）产生了兴趣，因为它可用于确定蛋白质的构象变化和对荧光共振能量转移（FRET）过程的敏感性。使用不同的光谱技术确定了 ANHP 在牛血清白蛋白（BSA）和人血清白蛋白（HSA）蛋白质环境中的位置。尽管在这两种情况下能量转移效率几乎相同，但结合常数值的差异促使我们在复杂的蛋白质环境中找到 ANHP 的位置。从 FRET 参数和α-螺旋性变化可以发现，ANHP 与 HSA 的色氨酸 214 和 BSA 的表面色氨酸 134 结合。在存在 ANHP 的情况下，HSA 中的蛋白质构象变化比 BSA 更为明显，这证实了 ANHP 在两种蛋白质环境中的位置。结合实验研究，还进行了分子对接分析，以解释 ANHP 在两种蛋白质中的位置和距离依赖的 FRET 过程。
