Shandong Key Laboratory of Water Pollution Control and Resource Reuse, School of Environmental Science and Engineering, Shandong University, China-America CRC for Environment & Health, Shandong Province, 27# Shanda South Road, Jinan 250100, PR China.
J Hazard Mater. 2011 Jun 15;190(1-3):574-81. doi: 10.1016/j.jhazmat.2011.03.084. Epub 2011 Mar 29.
4-Aminoantipyrine (AAP) is widely used in the pharmaceutical industry, in biochemical experiments and in environmental monitoring. AAP as an aromatic pollutant in the environment poses a great threat to human health. To evaluate the toxicity of AAP at the protein level, the effects of AAP on bovine serum albumin (BSA) were investigated by multiple spectroscopic techniques and molecular modeling. After the inner filter effect was eliminated, the experimental results showed that AAP effectively quenched the intrinsic fluorescence of BSA via static quenching. The number of binding sites, the binding constant, the thermodynamic parameters and binding subdomain were measured, and indicated that AAP could spontaneously bind with BSA on subdomain IIIA through electrostatic forces. Molecular docking results revealed that AAP interacted with the Glu 488 and Glu 502 residues of BSA. Furthermore, the conformation of BSA was demonstrably changed in the presence of AAP. The skeletal structure of BSA loosened, exposing internal hydrophobic aromatic ring amino acids and peptide strands to the solution.
4-氨基安替比林（AAP）在制药工业、生化实验和环境监测中被广泛应用。作为环境中的芳香族污染物，AAP 对人类健康构成了巨大威胁。为了在蛋白质水平上评估 AAP 的毒性，采用多种光谱技术和分子建模方法研究了 AAP 对牛血清白蛋白（BSA）的影响。在消除内滤效应后，实验结果表明，AAP 通过静态猝灭有效地猝灭了 BSA 的固有荧光。测量了结合位点数、结合常数、热力学参数和结合亚域，表明 AAP 可以通过静电力自发地与 BSA 的 IIIA 亚域结合。分子对接结果表明，AAP 与 BSA 的 Glu488 和 Glu502 残基相互作用。此外，在 AAP 的存在下，BSA 的构象明显发生变化。BSA 的骨架结构变松，暴露出内部疏水性芳环氨基酸和肽链到溶液中。
