Related Experiment Video
Updated: May 2, 2026
11:46
Extremely Rapid and Specific Metabolic Labelling of RNA In Vivo with 4-Thiouracil Ers4tU
Published on: August 22, 2019
13.2K
A protein engineered to bind uranyl selectively and with femtomolar affinity
Lu Zhou1, Mike Bosscher1, Changsheng Zhang2
11] Department of Chemistry and Institute for Biophysical Dynamics, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA [2].
Nature Chemistry
|February 22, 2014
Summary
Researchers engineered a uranyl-binding protein with high affinity and selectivity for uranium extraction from seawater. This breakthrough offers potential for biotechnology and environmental remediation applications.
Area of Science:
- Biotechnology
- Environmental Science
- Protein Engineering
Background:
- Uranyl (UO2(2+)) is the main form of uranium in aerobic environments, found in oceans at ~13.7 nM.
- Extracting uranyl from seawater is challenging due to similar metal ions, hindering selective binding motif design.
Purpose of the Study:
- To design and develop a uranyl-binding protein with high selectivity and affinity.
- To explore computational screening for identifying potential uranyl-binding sites.
Main Methods:
- Utilized computational screening to identify potential uranyl-binding sites.
- Engineered a thermally stable protein with specific uranyl-binding capabilities.
Main Results:
- The engineered protein exhibits extremely high affinity for uranyl (Kd = 7.4 fM).
- Achieved >10,000-fold selectivity for uranyl over other metal ions.
- Demonstrated repeated sequestration of 30-60% uranyl from synthetic seawater.
Conclusions:
- The developed uranyl-binding protein shows significant potential for uranium extraction from marine environments.
- The protein engineering strategy can be adapted for creating other selective metal-binding proteins.
- This approach has implications for biotechnology and environmental remediation efforts.
