A protein engineered to bind uranyl selectively and with femtomolar affinity

2014-03-01
Zhou, Lu
Bosscher, Mike
Zhang, Changsheng
Özçubukçu, Salih
Zhang, Liang
Zhang, Wen
Li, Charles J.
Liu, Jianzhao
Jensen, Mark P.
Lai, Luhua
He, Chuan
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.
NATURE CHEMISTRY

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Citation Formats
L. Zhou et al., “A protein engineered to bind uranyl selectively and with femtomolar affinity,” NATURE CHEMISTRY, pp. 236–241, 2014, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/39566.