Novel CRS Fragment Peptide Stability Without Affinity Tags
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Solution Overview
Problem
Existing CRS fragment peptides exhibit anticancer and immune-enhancing activities but face challenges in drug development due to stability issues and affinity tag requirements.
Innovation Solution
A novel CRS fragment peptide comprising consecutive amino acids from the 99th to the 140th and 185th to 228th amino acids in the amino acid sequence of SEQ ID NO: 1, or an amino acid sequence with 80% or more homology, is developed to maintain stability and efficacy without affinity tags.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If conventional CRS fragment peptides are used, then immune-enhancing activity is achieved, but stability at high temperatures deteriorates and affinity tags are required
Solution Approach 1:
The patent extracts and eliminates the affinity tag component from the conventional CRS fragment peptide system. By identifying and removing the affinity tag sequence while retaining the core immunopotentiating peptide sequence, the invention achieves stability without requiring external affinity tags for purification or stabilization.
Solution Approach 2:
The patent modifies the amino acid sequence parameters of the CRS fragment peptide by selecting specific consecutive amino acids from positions 101-140 to positions 200-228 in the human cysteinyl-tRNA synthetase sequence. This parameter change in the peptide structure confers high temperature stability and monomeric existence without requiring affinity tags.
2Reliability
If CRS fragment peptides are used for therapeutic applications, then anticancer and immune-enhancing activities are achieved, but unpredictability of biological effects worsens drug development
Solution Approach 1:
The patent segments the full-length cysteinyl-tRNA synthetase protein into a specific fragment containing consecutive amino acids from position 101-140 to 200-228. This segmentation isolates the therapeutically active region with predictable immunopotentiating activity while eliminating unpredictable biological effects associated with other regions of the full-length protein.
Solution Approach 2:
The patent applies local quality by concentrating the therapeutic activity in a specific local region of the cysteinyl-tRNA synthetase protein. The identified peptide sequence from positions 101-140 to 200-228 possesses enhanced local immunopotentiating properties that are more predictable and controllable than the full-length protein.
3Reliability
If existing CRS fragment peptides are used, then immune-enhancing activity is achieved, but degradation without affinity tags worsens
Solution Approach 1:
The patent extracts the essential immunopotentiating sequence from the conventional CRS fragment peptide and eliminates the unstable regions. By taking out only the necessary consecutive amino acids from positions 101-140 to 200-228, the invention creates a stable peptide that maintains immune-enhancing activity without requiring affinity tags for stabilization.
Solution Approach 2:
The patent creates a composite peptide structure by combining specific amino acid sequences from positions 101-140 to 200-228 of cysteinyl-tRNA synthetase with optimal structural characteristics. This composite sequence achieves both immune-enhancing activity and high stability without external stabilizing elements.
Data Source
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AI summary
The present invention relates to a novel CRS fragment peptide with immune-enhancing activity and its uses, more specifically to a novel peptide consisting of the amino acid sequence of SEQ ID NO:2 or an amino acid sequence having 95% or more sequence homology thereto, and its use as a vaccine adjuvant, an anticancer agent, and an antiviral composition. The peptide disclosed in the present invention is a CRS fragment disclosed for the first time in this specification, exhibiting anticancer activity, immune function enhancement, and antiviral activity.