A protein engineered to bind uranyl selectively and with femtomolar affinity

作者：Zhou, Lu; Bosscher, Mike; Zhang, Changsheng; Oezcubukcu, Salih; Zhang, Liang; Zhang, Wen; Li, Charles J.; Liu, Jianzhao; Jensen, Mark P.; Lai, Luhua^*; He, Chuan

来源：Nature Chemistry, 2014, 6(3): 236-241.

DOI：10.1038/NCHEM.1856

• COORDINATION CHEMISTRY
• ENZYME DESIGN
• SEA-WATER
• URANIUM
• EXTRACTION
• SEAWATER
• ION
• METALLOPROTEINS
• FORMS

Uranyl (UO22+), the predominant aerobic form of uranium, is present in the ocean at a concentration of similar to 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 K-d 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.

• 出版日期2014-3
• 单位北京大学; 分子动态与稳态结构国家重点实验室