A protein engineered to bind uranyl selectively and with femtomolar affinity View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2014-03

AUTHORS

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

ABSTRACT

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. More... »

PAGES

236-241

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nchem.1856

DOI

http://dx.doi.org/10.1038/nchem.1856

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1042973312

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24557139


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