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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Unraveling the binding interaction of a bioactive pyrazole-based probe with serum proteins: Relative concentration dependent 1:1 and 2:1 probe-protein stoichiometries
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Unraveling the binding interaction of a bioactive pyrazole-based probe with serum proteins: Relative concentration dependent 1:1 and 2:1 probe-protein stoichiometries

机译：揭开生物活性吡唑基探针与血清蛋白的结合相互作用：相对浓度依赖性1：1和2：1探针 - 蛋白质化学测定物

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摘要

Molecular interactions and binding of probes/drugs with biomacromolecular systems are of fundamental importance in understanding the mechanism of action and hence designing of proactive drugs. In the present study, binding interactions of a biologically potent fluorophore, (E)-1,5-diphenyl-3-styryl-4,5-dihydro-1H-pyrazole (DSDP) with two serum transport proteins, human serum albumin and bovine serum albumin, have been investigated exploiting multi-spectroscopic techniques. The spectrophotometric and fluorometric studies together with fluorescence quenching, fluorescence anisotropy, urea induced denaturation studies and fluorescence lifetime measurements reveal strong binding of DSDP with both the plasma proteins. Going beyond the vast literature data mostly providing 1:1 probe-protein complexation, the present investigation portrays 2:1 probe protein complex formation at higher relative probe concentration. A newer approach has been developed to have an estimate of the binding constants varying the concentration of the protein, instead of the usual practice of varying the probe. The binding constants for the 2:1 DSDP-protein complexes are determined to be 1.37 x 10(10)M(-2) and 1.47 x 10(10)M(-2) for HSA and BSA respectively, while those for the 1:1 complexation process come out to be 1.85 x 10(5)M(-2) and 1.73 x 10(5) M-1 for DSDP-HSA and DSDP-BSA systems respectively. Thermodynamic analysis at different temperatures implies that the forces primarily involved in the binding process are hydrogen bonding and hydrophobic interactions. Competitive replacement studies with known site markers and molecular docking simulations direct to the possible locations and binding energies of DSDP with the two serum proteins, corroborating well with the experimental results.
机译：探针/药物的分子相互作用和探针/药物的结合在理解行动机制和设计积极药物方面具有至关重要的重要性。在本研究中，具有两种血清转运蛋白，人血清白蛋白和牛的生物有效荧光团，（E）-1,5-二苯基-3-吡酰基-4,5-二氢-1H-吡唑（DSDP）的结合相互作用已经研究过利用多光谱技术进行血清白蛋白。分光光度和荧光性研究与荧光猝灭，荧光各向异性，尿素诱导的变性研究和荧光寿命测量结果揭示了DSDP与血浆蛋白质的强粘合。超出大多数提供1：1探针蛋白络合的广大文献数据，本研究表现出2：1探针蛋白质复合物浓度较高。已经开发了一种更新的方法，以估计改变蛋白质浓度的结合常数，而不是改变探针的通常实践。用于分别为HSA和BSA的2：1 DSDP-蛋白质复合物的结合常数为1.37×10（10）m（-2）和1.47×10（10）m（-2），而1 ：1分别为DSDP-HSA和DSDP-BSA系统的1.85×10（-2）和1.73×10（5）m-1的络合过程。不同温度的热力学分析意味着主要参与结合过程的力是氢键和疏水相互作用。具有已知的网站标记和分子对接模拟的竞争替代研究直接与两种血清蛋白质的可能位置和DSDP的结合能量，与实验结果均匀良好。

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