Dynorphin Peptide Analogues for Selective Opioid Receptor Binding
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Solution Overview
Problem
Current pain management drugs, such as opioids, have significant side effects like constipation, sedation, respiratory depression, dependence, and tolerance, and endogenous opioids like dynorphin have short metabolic stability, limiting their effectiveness and duration of action.
Innovation Solution
Development of peptide analogues of dynorphin with selective activity on opioid receptors and improved in vivo stability, formulated as compounds of specific structures and their pharmaceutically acceptable salts, solvates, stereoisomers, or prodrugs, for longer-lasting pain management with reduced side effects.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Object-affected harmful factors
If opioids are used for pain management, then pain relief is achieved, but side effects such as constipation, sedation, respiratory depression, dependence and tolerance occur
Solution Approach 1:
The patent applies local quality by designing peptide analogues with specific amino acid sequences that target particular opioid receptors (mu, delta, or kappa) with high selectivity. By optimizing the local chemical properties of the peptide structure, the invention achieves receptor-specific binding that produces analgesia while minimizing activation of receptors responsible for side effects.
Solution Approach 2:
The patent employs parameter changes by systematically modifying the amino acid composition and structure of dynorphin analogues. Specific substitutions at defined positions in the peptide sequence alter the pharmacological profile, enabling tuning of receptor selectivity, affinity, and metabolic stability to improve the therapeutic index.
2Duration of action of moving object
If dynorphin is used for analgesia, then pain relief is provided, but metabolic stability is poor resulting in short half-life
Solution Approach 1:
The patent applies parameter changes by systematically modifying the amino acid composition and structure of dynorphin analogues. Specific substitutions at defined positions in the peptide sequence alter the pharmacological profile, enabling tuning of receptor selectivity, affinity, and metabolic stability to improve the therapeutic index.
Solution Approach 2:
The patent employs composite materials by creating hybrid peptide structures that combine natural amino acid residues with non-natural or modified residues. These composite peptide analogues maintain the bioactive conformation necessary for receptor binding while incorporating structural features that resist enzymatic degradation, thereby extending in vivo half-life.
3Object-affected harmful factors
If selective opioid receptor activity is achieved, then side effects are reduced, but drug development complexity increases
Solution Approach 1:
The patent applies segmentation by dividing the opioid receptor family into distinct targets (mu, delta, kappa receptors) and designing peptide analogues that selectively bind to specific subtypes. This segmentation approach allows the invention to address side effects associated with non-selective opioid activation by targeting only the therapeutic receptor subtype.
Solution Approach 2:
The patent applies local quality by designing peptide analogues with specific amino acid sequences that target particular opioid receptors (mu, delta, or kappa) with high selectivity. By optimizing the local chemical properties of the peptide structure, the invention achieves receptor-specific binding that produces analgesia while minimizing activation of receptors responsible for side effects.
Data Source
AI summary
Peptide analogues of dynorphin and their use in pain management, the peptide analogues having good biological stability and reduced side effects compared to opioid analgesics.