A protein engineered to bind uranyl selectively and with femtomolar affinity. 2014

Lu Zhou, and Mike Bosscher, and Changsheng Zhang, and Salih Ozçubukçu, and Liang Zhang, and Wen Zhang, and Charles J Li, and Jianzhao Liu, and Mark P Jensen, and Luhua Lai, and Chuan He
1] Department of Chemistry and Institute for Biophysical Dynamics, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA [2].

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.

UI MeSH Term Description Entries
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D014501 Uranium A radioactive element of the actinide series of metals. It has an atomic symbol U, atomic number 92, and atomic weight 238.03. U-235 is used as the fissionable fuel in nuclear weapons and as fuel in nuclear power reactors.
D015202 Protein Engineering Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes. Genetic Engineering of Proteins,Genetic Engineering, Protein,Proteins, Genetic Engineering,Engineering, Protein,Engineering, Protein Genetic,Protein Genetic Engineering
D053768 Metal Nanoparticles Nanoparticles produced from metals whose uses include biosensors, optics, and catalysts. In biomedical applications the particles frequently involve the noble metals, especially gold and silver. Metal Nanocrystals,Metallic Nanocrystals,Metallic Nanoparticles,Metal Nanocrystal,Metal Nanoparticle,Metallic Nanocrystal,Metallic Nanoparticle,Nanocrystal, Metal,Nanocrystal, Metallic,Nanocrystals, Metal,Nanocrystals, Metallic,Nanoparticle, Metal,Nanoparticle, Metallic,Nanoparticles, Metal,Nanoparticles, Metallic

Related Publications

Lu Zhou, and Mike Bosscher, and Changsheng Zhang, and Salih Ozçubukçu, and Liang Zhang, and Wen Zhang, and Charles J Li, and Jianzhao Liu, and Mark P Jensen, and Luhua Lai, and Chuan He
January 2019, Frontiers in molecular biosciences,
Lu Zhou, and Mike Bosscher, and Changsheng Zhang, and Salih Ozçubukçu, and Liang Zhang, and Wen Zhang, and Charles J Li, and Jianzhao Liu, and Mark P Jensen, and Luhua Lai, and Chuan He
June 2023, Materials today. Bio,
Lu Zhou, and Mike Bosscher, and Changsheng Zhang, and Salih Ozçubukçu, and Liang Zhang, and Wen Zhang, and Charles J Li, and Jianzhao Liu, and Mark P Jensen, and Luhua Lai, and Chuan He
August 2008, Protein engineering, design & selection : PEDS,
Lu Zhou, and Mike Bosscher, and Changsheng Zhang, and Salih Ozçubukçu, and Liang Zhang, and Wen Zhang, and Charles J Li, and Jianzhao Liu, and Mark P Jensen, and Luhua Lai, and Chuan He
August 2018, Organic & biomolecular chemistry,
Lu Zhou, and Mike Bosscher, and Changsheng Zhang, and Salih Ozçubukçu, and Liang Zhang, and Wen Zhang, and Charles J Li, and Jianzhao Liu, and Mark P Jensen, and Luhua Lai, and Chuan He
December 2022, Inorganic chemistry,
Lu Zhou, and Mike Bosscher, and Changsheng Zhang, and Salih Ozçubukçu, and Liang Zhang, and Wen Zhang, and Charles J Li, and Jianzhao Liu, and Mark P Jensen, and Luhua Lai, and Chuan He
May 1995, Proceedings of the National Academy of Sciences of the United States of America,
Lu Zhou, and Mike Bosscher, and Changsheng Zhang, and Salih Ozçubukçu, and Liang Zhang, and Wen Zhang, and Charles J Li, and Jianzhao Liu, and Mark P Jensen, and Luhua Lai, and Chuan He
September 2012, Biochemistry,
Lu Zhou, and Mike Bosscher, and Changsheng Zhang, and Salih Ozçubukçu, and Liang Zhang, and Wen Zhang, and Charles J Li, and Jianzhao Liu, and Mark P Jensen, and Luhua Lai, and Chuan He
January 2016, PloS one,
Lu Zhou, and Mike Bosscher, and Changsheng Zhang, and Salih Ozçubukçu, and Liang Zhang, and Wen Zhang, and Charles J Li, and Jianzhao Liu, and Mark P Jensen, and Luhua Lai, and Chuan He
November 2004, Nature biotechnology,
Lu Zhou, and Mike Bosscher, and Changsheng Zhang, and Salih Ozçubukçu, and Liang Zhang, and Wen Zhang, and Charles J Li, and Jianzhao Liu, and Mark P Jensen, and Luhua Lai, and Chuan He
January 2012, PloS one,
Copied contents to your clipboard!