LanCL-Binding Peptide Composition for Broad-Spectrum Cell Stress Relief
Find Innovative SolutionsGenerate Solutions
Solution Overview
Problem
Existing peptide-based therapeutics are limited to treating specific diseases and conditions, lacking broad-spectrum activity for alleviating multiple diseases, conditions, or symptoms associated with ageing, damage, or stress to cells.
Innovation Solution
Development of peptides with a consensus amino acid sequence capable of binding to Lanthionine synthetase C-like (LanCL) protein, exhibiting analgesic, anti-inflammatory, and anti-microbial activity, irrespective of cyclic or linear configuration, with lengths ranging from 3 to 20 amino acids.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Adaptability or versatility
If existing peptide-based therapeutics are used, then specific disease treatment is achieved, but broad-spectrum activity for multiple conditions is lacking
Solution Approach 1:
The patent identifies a consensus amino acid sequence motif that serves as a universal binding element for LanCL protein across different therapeutic contexts. By designing peptides incorporating this conserved motif, a single peptide structure can simultaneously provide analgesic, anti-inflammatory, and anti-microbial activities, eliminating the need for multiple separate peptides to treat different conditions.
Solution Approach 2:
The patent varies parameters such as peptide length (3-20 amino acids), amino acid composition at non-critical positions, and cyclic vs linear configuration while maintaining the core consensus sequence. These parameter changes allow optimization of binding affinity and therapeutic activity without requiring fundamentally different peptide structures, thus achieving broad-spectrum activity with a limited set of related peptides.
2Adaptability or versatility
If peptides are designed to bind LanCL protein, then broad therapeutic effects are achieved, but peptide structure complexity increases
Solution Approach 1:
The patent segments the peptide structure into two functional regions: a conserved core motif that binds LanCL protein (providing the therapeutic effect) and variable flanking regions that can be optimized for stability, solubility, or pharmacokinetic properties. This segmentation allows the core binding function to remain simple and consistent while permitting complexity in other regions for enhanced performance.
Solution Approach 2:
The consensus sequence serves as a universal functional module that can be incorporated into different peptide backbones (cyclic or linear, different lengths) to achieve multiple therapeutic effects through a single design principle, reducing overall structural complexity.
3Strength
If peptide length is increased to improve binding affinity, then binding strength increases, but peptide stability and manufacturability decrease
Solution Approach 1:
The patent employs cyclic peptide structures where the peptide chain is connected at the N- and C-termini, creating a dynamic conformational constraint that stabilizes the binding motif. This cyclic structure maintains high binding affinity while improving proteolytic stability compared to linear peptides of equivalent length, as the cyclic structure resists degradation by proteases.
Solution Approach 2:
The patent uses disulfide bonds (flexible covalent links) to cyclize the peptide structure, creating a flexible yet stable scaffold that maintains the conserved motif in an optimal conformation for LanCL binding while protecting the peptide from degradation. The disulfide bridge provides structural stability without rigidifying the binding interface.
Data Source
AI summary
A peptide capable of binding to Lanthionine synthetase C-like (LanCL) protein, wherein the peptide comprises an amino acid sequence of formula (I):X1-X2-X3-X4-X5-X6 (I)wherein:(a) X1 is selected from the group consisting of lysine, arginine and histidine, or X1 is absent;(b) X2 is selected from the group consisting of alanine, valine, leucine, isoleucine, proline, phenylalanine, cysteine, tyrosine and serine;(c) X3 is selected from the group consisting of glycine, alanine, valine, leucine and isoleucine;(d) X4 is selected from the group consisting of serine, cysteine, threonine, asparagine, arginine, glutamine, tyrosine, aspartic acid, lysine, glutamic acid, proline and histidine, or X4 is absent;(e) X5 is selected from the group consisting of serine, cysteine, threonine, asparagine, arginine, glutamine, tyrosine, lysine, histidine and glycine, or X5 is absent; and(f) X6 is selected from the group consisting of serine, cysteine, threonine, asparagine, glutamine, tyrosine, and histidine, or X6 is absent,wherein the peptide is from 3 to 20 amino acids in length;wherein the amino acid sequence of the peptide does not comprise CRSRPVESSC (SEQ ID NO:13), CRSVEGSCG (SEQ ID NO:7), or CRIIHNNNC (SEQ ID NO:24); andwherein the peptide is not a linear peptide comprising the amino acid sequence EQLERALNSS (SEQ ID NO:65).