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首页> 外文期刊>Journal of biochemical and molecular toxicology >Toxic interaction between acid yellow 23 and trypsin: Spectroscopic methods coupled with molecular docking
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Toxic interaction between acid yellow 23 and trypsin: Spectroscopic methods coupled with molecular docking

机译：酸性黄23和胰蛋白酶之间的毒性相互作用：光谱方法与分子对接

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摘要

Acid yellow 23 (AY23) is a pervasive azo dye used in many fields which is potentially harmful to the environment and human health. This paper studied the toxic effects of AY23 on trypsin by spectroscopic and molecular docking methods. The addition of AY23 effectively quenched the intrinsic fluorescence of trypsin via static quenching with association constants of K 290,K = 3.67 × 10 5 L mol -1 and K 310,K = 1.83 × 10 5 L mol -1. The calculated thermodynamic parameters conformed that AY23 binds to trypsin predominantly via electrostatic forces with one binding site. Conformational investigations indicated the skeletal structure of trypsin unfolded and the microenvironment of tryptophan changed with the addition of AY23. Molecular docking study showed that AY23 interacted with the His 57 and Lys 224 residue of trypsin and led to the inhibition of enzyme activity. This study offers a more comprehensive picture of AY23-trypsin interaction and indicates their interaction may perform toxic effects within the organism.
机译：酸性黄23（AY23）是一种普遍使用的偶氮染料，可在许多领域中使用，对环境和人体健康有潜在危害。本文通过光谱和分子对接方法研究了AY23对胰蛋白酶的毒性作用。 AY23的添加通过静态猝灭有效地猝灭了胰蛋白酶的固有荧光，缔合常数为K 290，K = 3.67×10 5 L mol -1和K 310，K = 1.83×10 5 L mol -1。计算得到的热力学参数表明，AY23主要通过具有一个结合位点的静电力与胰蛋白酶结合。构象研究表明，随着AY23的加入，胰蛋白酶的骨架结构展开，色氨酸的微环境发生了变化。分子对接研究表明，AY23与胰蛋白酶的His 57和Lys 224残基相互作用，并导致酶活性受到抑制。这项研究提供了AY23-胰蛋白酶相互作用的更全面的图像，并表明它们的相互作用可能在生物体内产生毒性作用。

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