Ionic Self-Assembling Peptides Stable at Neutral pH

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Solution Overview

Problem

Existing self-assembling peptides require formulation at acidic or basic pH to remain soluble, leading to potential cell and tissue damage upon administration, and lack desirable physical properties under physiological conditions.

Innovation Solution

Development of ionic self-assembling peptides with specific amino acid combinations that maintain a non-zero net charge at neutral pH, allowing formulation and stability at physiological pH, forming hydrogels with shear-thinning, thixotropic, and rheological properties.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Stability of the object's composition

If self-assembling peptides with alternating positively and negatively charged residues are formulated at neutral pH, then the peptides exhibit self-assembling properties, but the peptides undergo phase separation and precipitation

Engineering Contradiction:

Improvepeptide stabilityVSAvoidformulation reliability

Core Design Contradiction:

Stability of the object's compositionVSReliability

Solution Approach 1:

The patent changes the charge distribution parameter of the peptide sequence from equal positive and negative charges to an imbalance (more positive than negative charges). This parameter change allows the peptides to maintain solubility and stability at neutral pH while retaining self-assembling capabilities, preventing phase separation and precipitation.

Inventive Principle:

Principle #35Parameter changes

2Stability of the object's composition

If self-assembling peptides are formulated at acidic pH to maintain solubility, then the peptides remain in solution, but the acidic pH causes cell and tissue damage upon administration

Engineering Contradiction:

Improvepeptide solubilityVSAvoidtissue damage

Core Design Contradiction:

Stability of the object's compositionVSObject-affected harmful factors

Solution Approach 1:

The patent modifies the peptide charge composition to have more positively charged residues than negatively charged residues. This parameter change enables the formulation to be adjusted to neutral pH (physiological condition) while maintaining peptide solubility through the net positive charge, thereby eliminating tissue damage associated with acidic formulations.

Inventive Principle:

Principle #35Parameter changes

3Stability of the object's composition

If self-assembling peptides have equivalent amounts of positive and negative charges, then the peptides can form stable assemblies, but the peptides require acidic or basic pH for formulation

Engineering Contradiction:

Improveassembly stabilityVSAvoidpH condition

Core Design Contradiction:

Stability of the object's compositionVSTemperature

Solution Approach 1:

The patent changes the charge ratio parameter from 1:1 (equal positive and negative charges) to an imbalanced ratio (more positive than negative charges). This parameter change allows the peptide assemblies to form and remain stable at neutral pH, eliminating the requirement for acidic or basic pH conditions.

Inventive Principle:

Principle #35Parameter changes

4Object-affected harmful factors

If self-assembling peptides are designed for neutral pH formulation, then the peptides can be administered without tissue damage, but the peptides exhibit phase separation and precipitation

Engineering Contradiction:

Improvetissue damageVSAvoidpeptide stability

Core Design Contradiction:

Object-affected harmful factorsVSStability of the object's composition

Solution Approach 1:

The patent modifies the peptide sequence to contain more positively charged residues than negatively charged residues. This parameter change provides a net positive charge at neutral pH that prevents phase separation and precipitation, thereby maintaining peptide stability and solubility under physiological conditions without causing tissue damage.

Inventive Principle:

Principle #35Parameter changes

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 peptides can be formulated at neutral pH without causing tissue damage and form hydrogels with advantageous physical characteristics for clinical, industrial, and research applications.

Implementation Method 1

self-assembling peptides having specific combinations of ionic polar amino acids, hydrophobic amino acids, and non-ionic polar amino acids... peptides having non-zero net charge at neutral pH

Methodology Applied

Scientific EffectElectrostatic interactions: Ion Repulsion/Attraction

Implementation Method 2

self-assembling peptides... upon gelation, the self-assembling peptides may form hydrogels having shear-thinning, thixotropic, and rheological properties

Methodology Applied

Scientific EffectSelf-assembly: Self-Assembly