1] Department of Chemistry and Institute for Biophysical Dynamics, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA [2].
1] BNLMS, State Key Laboratory for Structural Chemistry of Unstable and Stable Species, College of Chemistry and Molecular Engineering and Center for Quantitative Biology, Peking University, Beijing 100871, China [2] Center for Life Sciences, Peking University, Beijing 100871, China [3].
Nat Chem. 2014 Mar;6(3):236-41. doi: 10.1038/nchem.1856. Epub 2014 Jan 26.
Uranyl (UO2(2+)), the predominant aerobic form of uranium, is present in the ocean at a concentration of ~3.2 parts per 10(9) (13.7 nM); however, the successful enrichment of uranyl from this vast resource has been limited by the high concentrations of metal ions of similar size and charge, which makes it difficult to design a binding motif that is selective for uranyl. Here we report the design and rational development of a uranyl-binding protein using a computational screening process in the initial search for potential uranyl-binding sites. The engineered protein is thermally stable and offers very high affinity and selectivity for uranyl with a Kd of 7.4 femtomolar (fM) and >10,000-fold selectivity over other metal ions. We also demonstrated that the uranyl-binding protein can repeatedly sequester 30-60% of the uranyl in synthetic sea water. The chemical strategy employed here may be applied to engineer other selective metal-binding proteins for biotechnology and remediation applications.
铀酰（UO2(2+)）是铀的主要有氧形式，其在海洋中的浓度约为 3.2 份/10(9)（13.7 nM）；然而，由于具有相似大小和电荷的金属离子浓度很高，成功地从这一巨大资源中富集铀酰受到了限制，这使得设计对铀酰具有选择性的结合基序变得困难。在这里，我们报告了一种使用计算筛选过程设计和合理开发铀酰结合蛋白的情况，该筛选过程是在最初寻找潜在铀酰结合位点的过程中进行的。该工程蛋白具有热稳定性，对铀酰具有非常高的亲和力和选择性，Kd 为 7.4 飞摩尔（fM），对其他金属离子的选择性超过 10,000 倍。我们还证明，铀酰结合蛋白可以反复螯合合成海水中 30-60%的铀酰。这里采用的化学策略可用于工程设计其他用于生物技术和修复应用的选择性金属结合蛋白。
