Charged Peptide Hydrogel Adjuvant for Antigen Retention
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Solution Overview
Problem
Current immunogenic compositions fail to effectively enhance the immunogenicity of various antigens, particularly those with positive charges at physiological pH, using self-assembling peptides without charges.
Innovation Solution
A peptide hydrogel composition containing positively or negatively charged self-assembling peptides, not covalently bonded to antigens, is developed, which includes a peptide with specific amino acid sequences and charges, enhancing antigen retention and immune response.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If uncharged self-assembling peptides are used as adjuvants, then the peptide can self-assemble to form nanofibers and hydrogels, but the immunogenicity enhancement is insufficient especially for positively charged antigens
Solution Approach 1:
The patent changes the charge parameter of the self-assembling peptide from uncharged to charged (positive or negative). This parameter change enables the peptide to interact electrostatically with antigens having opposite charges, thereby enhancing immunogenicity enhancement capability and compatibility with various antigen types, especially positively charged antigens.
2Stability of the object's composition
If the self-assembling peptide is covalently bonded to the antigen, then the antigen retention is improved, but the peptide loses its self-assembly capability and hydrogel formation
Solution Approach 1:
The patent uses non-covalent interactions (electrostatic interactions, hydrogen bonds, hydrophobic interactions) as intermediaries between the self-assembling peptide and the antigen. These intermediary forces are sufficient to retain the antigen on the peptide hydrogel structure without requiring covalent bonding, thus maintaining both antigen retention and peptide self-assembly capability.
Solution Approach 2:
The patent creates a composite structure where the self-assembling peptide forms a hydrogel matrix that physically traps and presents the antigen. This composite approach allows the peptide to maintain its self-assembly function while the antigen is retained through physical incorporation into the hydrogel network, avoiding covalent modification of the peptide.
3Strength
If the peptide concentration is increased to improve antigen retention, then the hydrogel strength increases, but the immunogenicity enhancement becomes less specific and more background noise
Solution Approach 1:
The patent optimizes the peptide concentration parameter to a specific range (0.1-5.0 w/v%) where the hydrogel achieves sufficient strength for antigen retention while maintaining high immunogenicity enhancement specificity. This parameter optimization ensures that the peptide concentration is high enough to form a stable hydrogel structure but not so high as to create non-specific background effects.
Applied Scientific Principles
This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.
Function Achieved in This Case
The composition significantly increases the immunogenicity of antigens by maintaining antigen presentation over time, as demonstrated by increased antibody production and immune response in animal models.
Implementation Method 1
A self-assembling peptide is a peptide that can spontaneously assemble in an aqueous solution through an interaction between peptide molecules to form a nanofiber
Implementation Method 2
a peptide hydrogel containing a positively or negatively charged self-assembling peptide and an aqueous medium
Data Source
AI summary
Provided is an immunogenic composition which contains a self-assembling peptide as an adjuvant and can increase the immunogenicity of various antigens. The present invention provides an immunogenic composition including: a peptide hydrogel containing a positively or negatively charged self-assembling peptide and an aqueous medium; and an antigen, in which the self-assembling peptide is not covalently bonded to the antigen.