黄曲霉毒素 B <sub>1</sub>诱导牛血清白蛋白的结构和构象变化：基于多光谱和圆二色性的研究,ACS Omega

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黄曲霉毒素 B ₁诱导牛血清白蛋白的结构和构象变化：基于多光谱和圆二色性的研究
ACS Omega ( IF 3.7 ) Pub Date : 2021-07-08 , DOI: 10.1021/acsomega.1c01799
Mohd Aamir Qureshi ₁ , Saleem Javed ₁

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黄曲霉毒素 B ₁ (AFB ₁ ) 是一种诱变剂，已被国际癌症研究机构归类为 1 类人类致癌物。它是由土壤真菌黄曲霉和寄生曲霉的次生代谢产物产生的。在这里，在本研究中，使用荧光光谱、紫外-可见吸收光谱和圆二色光谱偏振法等多光谱工具确定了 AFB ₁对牛血清白蛋白 (BSA) 结构和构象的影响。紫外吸收光谱揭示了在 AFB ₁存在下 BSA 吸收光谱的增色性. 通过荧光光谱法计算出的结合常数在 10 ⁴ M ^–1的范围内，表明毒素与 BSA 有适度结合。该研究还证实了荧光猝灭的静态性质。发现结合位点的化学计量是统一的。根据位点标记置换试验计算，华法林对 AFB ₁的竞争能力高于布洛芬。Förster 共振能量转移证实了从 BSA 到 AFB ₁的高效率能量转移。圆二色性分光偏振法显示在 AFB ₁存在下 BSA 中的 α-螺旋减少. 在存在霉菌毒素的情况下，BSA 的熔解温度从 62.5 °C 增加到 70.3 °C。分子对接证实了 AFB ₁与 BSA 中亚域 IIA的结合。

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Aflatoxin B1 Induced Structural and Conformational Changes in Bovine Serum Albumin: A Multispectroscopic and Circular Dichroism-Based Study

Aflatoxin B₁ (AFB₁) is a mutagen that has been categorized as a group 1 human carcinogen by the International Agency for Research on Cancer. It is produced as a secondary metabolite by soil fungi Aspergillus flavus and Aspergillus parasiticus. Here, in this study, the effect of AFB₁ on the structure and conformation of bovine serum albumin (BSA) using multispectroscopic tools like fluorescence spectroscopy, ultraviolet–visible absorption spectroscopy, and circular dichroism spectropolarimetry has been ascertained. Ultraviolet absorption spectroscopy revealed hyperchromicity in the absorption spectra of BSA in the presence of AFB₁. The binding constant was calculated in the range of 10⁴ M^–1, by fluorescence spectroscopy suggesting moderate binding of the toxin to BSA. The study also confirms the static nature of fluorescence quenching. The stoichiometry of binding sites was found to be unity. The competing capability of warfarin for AFB₁ was higher than ibuprofen as calculated from site marker displacement assay. Förster resonance energy transfer confirmed the high efficiency of energy transfer from BSA to AFB₁. Circular dichroism spectropolarimetry showed a decrease in the α-helix in BSA in the presence of AFB₁. The melting temperature of BSA underwent an increment in the presence of a mycotoxin from 62.5 to 70.3 °C. Molecular docking confirmed the binding of AFB₁ to subdomain IIA in BSA.

更新日期：2021-07-20

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