Human serum albumin (HSA) is the most abundant plasma protein, which functions to transport a large range of ligands within the circulation. These interactions have important implications for human health and disease. The primary binding site for Cu^II ions on HSA is known to be the so-called amino-terminal Cu^II and Ni^II binding (ATCUN) motif. However, the number and identity of secondary binding sites is currently not understood. In this study, we harnessed a suite of contemporary electron paramagnetic resonance (EPR) spectroscopy methods to investigate recombinantly produced constructs of HSA bearing single-histidine knockouts, with the aim to characterise its endogenous Cu^II ion binding sites.

中文翻译：

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人血清白蛋白中天然 CuII 结合位点的 EPR 光谱表征


人血清白蛋白 (HSA) 是最丰富的血浆蛋白，其功能是在循环中运输大量配体。这些相互作用对人类健康和疾病具有重要影响。 HSA 上 Cu ^II 离子的主要结合位点是所谓的氨基末端 Cu ^II 和 Ni ^II 结合 (ATCUN) 基序。然而，目前尚不清楚第二结合位点的数量和身份。在这项研究中，我们利用一套现代电子顺磁共振 (EPR) 光谱方法来研究重组产生的带有单组氨酸敲除的 HSA 构建体，目的是表征其内源性 Cu ^II 离子结合位点。