The State Key Lab of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou, Fujian, 350002, People's Republic of China.
Environ Sci Pollut Res Int. 2014;21(11):6994-7005. doi: 10.1007/s11356-014-2610-8. Epub 2014 Feb 14.
Cadmium (Cd) is an extremely toxic metal commonly found as an environmental contaminant from industrial and agricultural sources, posing severe risks to human health. In this study, the binding mechanism of Cd(II)-human serum albumin (HSA) complex and the effect of Cd(II) on the conformational stability and structural state of HSA were comprehensively investigated through a series of efficient and appropriate methods. X-ray photoelectron spectroscopy accurately described the microenvironmental changes around protein C, N, and O atoms in the presence of Cd(II). Fluorescence results indicated that the probable mechanism of Cd(II)-HSA interaction is a static quenching process. Fourier transform infrared spectroscopy and dynamic light scattering showed Cd(II) complexation altered HSA conformation and the microenvironments of Trp and Tyr residues, accompanied by the size increases of HSA aggregates. This research will be helpful for understanding the toxic effects of Cd(II) on protein function in vivo.
镉（Cd）是一种极其有毒的金属，通常作为工业和农业来源的环境污染物存在，对人类健康构成严重威胁。在这项研究中，通过一系列高效和适当的方法，全面研究了 Cd(II)-人血清白蛋白（HSA）复合物的结合机制以及 Cd(II)对 HSA 构象稳定性和结构状态的影响。X 射线光电子能谱准确描述了 Cd(II)存在时蛋白质 C、N 和 O 原子周围微环境的变化。荧光结果表明，Cd(II)-HSA 相互作用的可能机制是静态猝灭过程。傅里叶变换红外光谱和动态光散射表明，Cd(II)络合改变了 HSA 的构象以及色氨酸和酪氨酸残基的微环境，同时 HSA 聚集体的尺寸增大。这项研究将有助于理解 Cd(II)对体内蛋白质功能的毒性作用。
