Iridium-Binding Peptide Sequence and Biotin-PEG Modification
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Solution Overview
Problem
There is a need for a novel peptide capable of binding to iridium, as existing peptides do not effectively recognize or interact with this element.
Innovation Solution
A peptide with a specific amino acid sequence (SQMMGHMGHGNMNHMNHGGKFDFHH) is developed, which is derived from the amino acid sequence of CueO, a multi-copper oxidase from Escherichia coli K-12, and is chemically modified with biotin-polyethylene glycol to enhance its binding capabilities to iridium nanoparticles.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If existing peptides are used, then the peptide structure is simple, but the binding ability to iridium is insufficient
Solution Approach 1:
The patent modifies the peptide sequence parameters by incorporating specific amino acid residues (His, Met, Cys) at defined positions to enhance iridium binding affinity. The sequence SQMMGHMGHGNMNHMNHGGKFDFHH contains strategically placed metal-binding residues that change the chemical properties of the peptide to improve iridium interaction
Solution Approach 2:
The patent creates a composite structure by combining the peptide with biotin-polyethylene glycol modification. This composite approach integrates the iridium-binding peptide sequence with biotin for potential avidin-mediated applications, enhancing both binding capability and functional versatility
2Reliability
If the peptide is chemically modified with biotin-polyethylene glycol, then the binding capability to iridium is enhanced, but the manufacturing process becomes more complex
Solution Approach 1:
The peptide sequence is designed with pre-positioned amino acid residues (His, Met, Cys) that are optimized for iridium binding before any chemical modification occurs. This preliminary optimization of the core sequence ensures high binding affinity is achieved at the design stage, reducing the complexity burden of subsequent biotin-PEG modification
Solution Approach 2:
The biotin-polyethylene glycol acts as an intermediary modification that attaches to the N-terminus of the peptide without interfering with the iridium-binding residues. This modular approach allows the binding function and the modification function to be separated, simplifying the overall manufacturing strategy
Data Source
AI summary
The present invention provides a novel peptide capable for binding to iridium. The peptide consists of an amino acid sequence represented by SQMMGHMGHGNMNHMNHGGKFDFHH (SEQ ID NO: 01).


