Uranium is an element belonging to the actinide series. It is ubiquitous in rock, soil, and water. Uranium is found in the ecosystem due to mining and milling industrial activities and processing to nuclear fuel, but also to the extensive use of phosphate fertilizers. Understanding uranium binding in vivo is critical, first to deepen our knowledge of molecular events leading to chemical toxicity, but also to provide new mechanistic information useful for the development of efficient decorporation treatments to be applied in case of intoxication. The most stable form in physiological conditions is the uranyl cation (UO22+), in which uranium oxidation state is +VI. This short review presents uranyl coordination properties and chelation, and what is currently known about uranium binding to proteins. Although several target proteins have been identified, the UO22+ binding sites have barely been identified. Biomimetic approaches using model peptides are good options to shed light on high affinity uranyl binding sites in proteins. A strategy based on constrained cyclodecapeptides allowed recently to propose a tetraphosphate binding site for uranyl that provides an affinity similar to the one measured with the phosphoprotein osteopontin.

中文翻译：

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由于仿生肽，蛋白质中铀酰结合的最新进展。

铀是属于the系元素的元素。它在岩石，土壤和水中无处不在。在铀矿生态系统中发现铀的原因是采矿和制粉工业活动以及向核燃料的加工，也归因于磷酸盐肥料的广泛使用。理解铀在体内的结合至关重要，首先是要加深我们对导致化学毒性的分子事件的了解，而且还应提供新的机械信息，以开发可用于中毒的有效脱附治疗方法。在生理条件下最稳定的形式是铀酰阳离子（UO22 +），其中铀的氧化态为+ VI。这篇简短的综述介绍了铀酰的配位性能和螯合作用，以及目前有关铀与蛋白质结合的已知信息。尽管已鉴定出几种靶蛋白，但几乎未鉴定出UO22 +结合位点。使用模型肽的仿生方法是阐明蛋白质中高亲和力铀酰结合位点的良好选择。基于受约束的环十肽的策略最近允许提出针对铀酰的四磷酸结合位点，其提供的亲和力类似于用磷蛋白骨桥蛋白测得的亲和力。