RAS Peptide Vaccine Composition for Broad HLA Immunogenicity

Resolve Bottlenecks,
Find Innovative SolutionsGenerate Solutions

Solution Overview

Problem

Existing peptide vaccines lack effectiveness due to the diversity of human MHC alleles and individual variability in immunogenicity, making it difficult to predict and target foreign peptides displayed by HLA molecules for cancer treatment or pathogen prevention.

Innovation Solution

Designing peptide vaccines that incorporate heteroclitic modifications to enhance peptide-HLA binding affinity and considering HLA allelic frequencies and linkage disequilibrium, using computational methods like OptiVax-Robust and OptiVax-Unlinked to select a diverse set of peptides for robust display across populations.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If peptide vaccines are designed to target specific HLA alleles, then immunogenicity for those alleles is improved, but coverage across diverse HLA populations deteriorates

Engineering Contradiction:

ImproveimmunogenicityVSAvoidHLA population coverage

Core Design Contradiction:

ReliabilityVSAdaptability or versatility

Solution Approach 1:

The vaccine design segments the HLA population into distinct allele groups and selects representative peptides for each segment. This allows targeted optimization for specific HLA alleles while maintaining overall population coverage through the segmented approach.

Inventive Principle:

Principle #1Segmentation

Solution Approach 2:

The invention changes the parameter of peptide selection by using computational algorithms (OptiVax-Robust, OptiVax-Unlinked) to identify peptides with optimized binding affinity across multiple HLA alleles. This parameter optimization resolves the contradiction by finding peptides that work across diverse alleles.

Inventive Principle:

Principle #35Parameter changes

2Adaptability or versatility

If a diverse set of peptides is selected to cover multiple HLA alleles, then HLA population coverage is improved, but vaccine complexity deteriorates

Engineering Contradiction:

ImproveHLA population coverageVSAvoidvaccine composition

Core Design Contradiction:

Adaptability or versatilityVSDevice complexity

Solution Approach 1:

The vaccine design seeks universal peptides that can bind to multiple HLA alleles simultaneously. This multi-functionality approach allows a single peptide to serve multiple HLA types, reducing the total number of peptides needed while maintaining broad population coverage.

Inventive Principle:

Principle #6Universality (Multi-functionality)

Solution Approach 2:

The computational algorithms identify a core set of high-priority peptides that provide the majority of population coverage. This partial action approach focuses resources on the most impactful peptides rather than attempting to cover every possible HLA allele equally.

Inventive Principle:

Principle #16Partial or excessive action

3Strength

If heteroclitic modifications are introduced to enhance peptide-HLA binding affinity, then binding strength is improved, but peptide sequence complexity deteriorates

Engineering Contradiction:

Improvepeptide-HLA binding affinityVSAvoidpeptide sequence design

Core Design Contradiction:

StrengthVSDevice complexity

Solution Approach 1:

Heteroclitic modifications are introduced at specific local positions within the peptide sequence rather than throughout the entire peptide. This localized modification approach enhances binding affinity at critical anchor positions while maintaining the overall peptide structure and minimizing complexity.

Inventive Principle:

Principle #3Local quality

Data Source

PatentUS20260000743A1Immunogenic compositions comprising nucleic acids for ras peptides

Publication Date: 2026.01.01 THINK THERAPEUTICS INC

AI summary

The present disclosure provides for methods, systems, and compositions of nucleic acid and peptide sequences. For example, the present disclosure provides for one or more polynucleotide sequences encoding one or more amino acid sequences selected from the group consisting of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 21, SEQ ID NO: 23, SEQ ID NO: 86, SEQ ID NO: 88, SEQ ID NO: 125, SEQ ID NO: 154, SEQ ID NO: 194, SEQ ID NO: 200, SEQ ID NO: 209, and SEQ ID NO: 366.