SRRD Protein Inhibiting Neurodegenerative Aggregation

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Solution Overview

Problem

Current therapies for neurodegenerative diseases such as Alzheimer's, Parkinson's, and ALS are inadequate in addressing protein aggregation, which is a hallmark of these conditions, leading to significant challenges in treatment and disease progression.

Innovation Solution

The use of SRR1 domain-containing protein (SRRD) or its active fragment, which can be delivered to cells via expression constructs or carriers like liposomes or nanoparticles, to reduce protein aggregation by overexpressing the protein or fragment, potentially delaying disease progression.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If current therapies are used to treat neurodegenerative diseases, then some symptoms may be managed, but protein aggregation remains unchecked and disease progression continues

Engineering Contradiction:
Improvedisease treatment effectivenessVSAvoidprotein aggregation
Core Design Contradiction:
ReliabilityVSObject-generated harmful factors

Solution Approach 1:

The patent identifies SRRD, a protein that naturally binds to and stabilizes misfolded proteins, converting a potentially harmful aggregation process into a beneficial stabilization mechanism. By leveraging the natural chaperone activity of SRRD, the patent transforms the cell's own protein folding machinery into a therapeutic advantage, where SRRD acts as a molecular chaperone that prevents aggregation of pathogenic proteins like TDP-43 and alpha-synuclein.

Inventive Principle:
Principle #22Blessing in disguise (Convert harm into benefit)

Solution Approach 2:

SRRD serves as an intermediary molecule between the cell's protein synthesis machinery and the degradation pathways. It acts as a molecular mediator that binds to misfolded proteins, preventing their aggregation while facilitating their proper folding or targeted degradation, thus serving as a protective intermediate that bridges multiple cellular processes.

Inventive Principle:
Principle #24Intermediary (Mediator)

2Object-affected harmful factors

If protein aggregation is not properly controlled, then tissue function is impaired, but the underlying mechanisms remain unclear

Engineering Contradiction:
Improvetissue function impairmentVSAvoidmechanism understanding
Core Design Contradiction:
Object-affected harmful factorsVSLoss of information

Solution Approach 1:

The patent demonstrates that SRRD provides self-service protection against protein aggregation through its intrinsic chaperone activity. The protein automatically binds to misfolded proteins and facilitates their proper folding or degradation without requiring external intervention or complex regulatory mechanisms, thereby protecting tissue function through a simple, self-active mechanism.

Inventive Principle:
Principle #25Self-service

3Object-generated harmful factors

If SRRD is overexpressed in cells, then protein aggregation is reduced, but the delivery mechanism becomes more complex

Engineering Contradiction:
Improveprotein aggregationVSAvoiddelivery mechanism
Core Design Contradiction:
Object-generated harmful factorsVSDevice complexity

Solution Approach 1:

The patent employs universal delivery mechanisms such as liposomes and nanoparticles that can transport SRRD across different cell types and tissue barriers. These multi-functional delivery systems can administer SRRD to various targets including neurons, glial cells, and other tissues, providing broad applicability across different neurodegenerative disease models without requiring disease-specific delivery systems.

Inventive Principle:
Principle #6Universality (Multi-functionality)

Data Source

PatentUS20220227824A1Use of SRRD in the inhibition of protein aggregation
Publication Date: 2022.07.21 THE CHILDRENS HOSPITAL OF PHILADELPHIA
  • US20220227824A1 patent drawing
  • US20220227824A1 patent drawing
  • US20220227824A1 patent drawing

AI summary

The present disclosure is directed to the use of SRR1 domain-containing protein (SRRD) or active fragment thereof to reduce protein aggregation, such as that occurring in neurodegenerative diseases.