Recombinant Silk-Elastin Protein Polymers for Controlled Drug Release

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Solution Overview

Problem

Current methods for delivering nucleic acids and bioactive agents in vivo face challenges in achieving safe and efficient localized delivery, with traditional chemical synthetic polymers producing random copolymers and natural polymers lacking control over release and mechanical properties, leading to variability and potential toxicity.

Innovation Solution

The use of recombinantly synthesized silk-elastin-like protein polymers with engineered protease cleavage sites, such as MMP-responsive sequences, to create controlled release systems for bioactive agents, allowing precise localization and sustained delivery in response to specific protease levels.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Manufacturing precision

If traditional chemical synthetic polymers are used for drug delivery, then manufacturing is easier and cost is lower, but the polymers produce random copolymers with poor control over release and mechanical properties

Engineering Contradiction:
Improvecontrol over release and mechanical propertiesVSAvoidmanufacturing complexity
Core Design Contradiction:
Manufacturing precisionVSEase of manufacture

Solution Approach 1:

The patent changes the manufacturing approach from chemical synthesis to recombinant DNA technology, enabling precise control over polymer structure, sequence, and properties while maintaining scalability through biological production systems

Inventive Principle:
Principle #35Parameter changes

Solution Approach 2:

The patent creates hybrid protein polymers combining silk and elastin sequences with integrated drug delivery functionality, achieving multiple controlled properties (release kinetics, mechanical strength, biodegradability) within a single recombinant material system

Inventive Principle:
Principle #40Composite materials

2Reliability

If natural polymers are used for drug delivery, then biocompatibility is improved, but control over release and mechanical properties is lost leading to variability

Engineering Contradiction:
Improveconsistency of release and mechanical propertiesVSAvoidcontrol over release and mechanical properties
Core Design Contradiction:
ReliabilityVSAdaptability or versatility

Solution Approach 1:

The patent introduces specific functional domains (MMP-responsive sequences, drug binding sites, structural elements) at defined locations within the polymer chain, enabling localized control over degradation, release, and mechanical properties while maintaining overall biocompatibility

Inventive Principle:
Principle #3Local quality

Solution Approach 2:

The patent divides the polymer into functional segments (silk domains for structure, elastin domains for flexibility, MMP-responsive sequences for controlled release) that can be independently optimized and recombined to achieve desired properties

Inventive Principle:
Principle #1Segmentation

3Ease of operation

If protease cleavage sites are engineered into the polymers, then controlled release in response to protease levels is achieved, but the polymer structure becomes more complex

Engineering Contradiction:
Improvecontrolled release capabilityVSAvoidpolymer structure complexity
Core Design Contradiction:
Ease of operationVSDevice complexity

Solution Approach 1:

The patent incorporates MMP-responsive sequences that automatically respond to the tumor microenvironment's protease levels, enabling self-regulated drug release without external control mechanisms or complex delivery systems

Inventive Principle:
Principle #25Self-service

Solution Approach 2:

The patent uses MMP-responsive sequences as intermediary elements that translate the biological signal (protease presence) into a functional response (polymer degradation and drug release), bridging the gap between tumor microenvironment and therapeutic action

Inventive Principle:
Principle #24Intermediary (Mediator)

4Duration of action of moving object

If localized delivery is achieved, then therapeutic efficacy is improved, but the need for multiple injections increases

Engineering Contradiction:
Improveduration of therapeutic effectVSAvoidnumber of injections required
Core Design Contradiction:
Duration of action of moving objectVSEase of operation

Solution Approach 1:

The patent loads the polymer with therapeutic agents during manufacturing, creating a pre-loaded delivery system that provides sustained release over time, eliminating the need for repeated administrations

Inventive Principle:
Principle #10Preliminary action

Solution Approach 2:

The patent designs the polymer to provide continuous therapeutic action through sustained release mechanisms, maintaining effective drug concentrations over extended periods without interruption or need for re-dosing

Inventive Principle:
Principle #20Continuity of useful action

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

This approach enhances the efficacy and safety of bioactive agent delivery by providing controlled, localized release of therapeutic agents, reducing toxicity and the need for multiple injections, while improving therapeutic outcomes and patient compliance.

Implementation Method 1

Matrix metalloproteinase cleavable protein polymers for cancer gene therapy

Methodology Applied
Scientific EffectProtease cleavage: Enzyme

Data Source

PatentEP2861732B1Matrix metalloproteinase cleavable protein polymers for cancer gene therapy
Publication Date: 2019.06.19 UNIV OF UTAH RES FOUND
  • EP2861732B1 patent drawingFigure 1~2
  • EP2861732B1 patent drawingFigure 3
  • EP2861732B1 patent drawingFigure 4A~4C

AI summary

A delivery system that includes a recombinantly synthesized protein polymer with protease cleavage sites such as matrix metalloproteinase responsive sequences engineered within the protein polymer. The system may be used to treat cancer, wounds, or pathological conditions in other tissues that express excess protease relative to healthy tissue.