Engineered Polypeptides for Selective Uranyl Ion Binding
Find Innovative SolutionsGenerate Solutions
Solution Overview
Problem
Current methods for selective binding and enrichment of uranyl ions from seawater face challenges due to competition from other metal ions and natural ligands, limiting efficient uranium extraction and remediation.
Innovation Solution
Engineered recombinant polypeptides with specific amino acid sequences, such as those at least 80% identical to SEQ ID NOs: 1, 3, 5, 7, or 9, are designed to selectively bind uranyl ions with high affinity and stability, allowing for efficient uranium extraction and remediation from seawater.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If conventional methods are used for binding uranyl ions, then binding capacity is achieved, but selectivity is reduced due to competition from other metal ions and natural ligands
Solution Approach 1:
The patent applies local quality by designing specific amino acid residues at precise positions within the protein scaffold to create a localized binding site with optimized chemical properties. The binding site contains negatively charged residues (Asp, Glu) positioned to coordinate with uranyl ions, while other regions of the protein maintain structural stability without interfering with binding selectivity
Solution Approach 2:
The patent employs parameter changes by systematically varying amino acid sequences at key positions (such as positions 13, 17, 64, 67) to optimize binding affinity and selectivity. By changing charge distribution, hydrophobicity, and steric properties at specific locations, the protein achieves femtomolar dissociation constants while maintaining resistance to competition from other metal ions
2Reliability
If protein scaffolds are engineered for high selectivity, then binding affinity increases, but structural stability may be compromised
Solution Approach 1:
The patent applies segmentation by dividing the protein into distinct functional regions: a structured core domain that provides structural stability and a surface-exposed binding site that provides selective affinity. This modular design allows independent optimization of stability and binding properties without compromising either function
Solution Approach 2:
The patent uses composite materials by combining naturally derived protein scaffolds with rationally designed amino acid sequences. The natural scaffold provides structural framework and stability, while engineered residues introduce high-affinity binding characteristics, creating a composite structure that exhibits both stability and high binding affinity
Applied Scientific Principles
This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.
Function Achieved in This Case
The engineered polypeptides demonstrate high selectivity and stability, enabling the extraction of uranyl ions from seawater with dissociation constants in the femtomolar range, facilitating economic uranium mining and environmental remediation.
Implementation Method 1
specifically bind to actinide and/or lanthanide oxides, such as uranyl
Implementation Method 2
amino acid sequence comprises one or more of the following features (a) an amino acid with a negatively charged side chain (e.g., Asp or Glu) at the position corresponding to Asn 13 of SEQ ID NO: 1
Data Source
AI summary
Polypeptides comprising high affinity for the uranyl ion are provided. Methods for binding uranyl using such proteins are likewise provided and can be used, for example, in methods for uranium purification or removal.