Secretory sDSS1 Protein Conjugates Pathogenic Proteins
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Solution Overview
Problem
Current methods are inadequate in effectively preventing and treating diseases caused by excessive formation or accumulation of junk proteins, such as chronic kidney disease, Alzheimer's, and diabetes complications, as they fail to efficiently manage the removal and aggregation of oxidized, glycosylated, and amyloid proteins.
Innovation Solution
A secretory subtype of the DSS1 protein (sDSS1) is developed, which can be secreted into blood and cerebrospinal fluid, forming conjugates with oxidized and amyloid proteins without energy-consuming enzymatic reactions, thereby reducing their cytotoxicity and promoting their degradation.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If conventional methods are used to remove junk proteins, then the organism's existing mechanisms are utilized, but they become inadequate during aging or disease when excessive junk proteins accumulate
Solution Approach 1:
The sDSS1 protein acts as an intermediary substance that facilitates the removal of junk proteins. It binds to oxidized proteins, glycated proteins, and amyloid proteins through its specific binding sites, forming complexes that can be efficiently cleared from the body, thereby enhancing the organism's natural protein removal mechanisms.
Solution Approach 2:
The invention introduces a new protein parameter - the secretory DSS1 protein with specific amino acid sequence and structure - that changes the capacity and efficiency of the protein removal system. This new parameter enables the system to handle excessive junk protein accumulation that conventional mechanisms cannot manage.
2Reliability
If drugs are used to block protein aggregation, then pathogenic protein formation is reduced, but the complexity of drug development and administration increases
Solution Approach 1:
The sDSS1 protein performs its protective function automatically by binding to pathogenic proteins and preventing their aggregation. This self-service mechanism eliminates the need for complex drug formulations, administration protocols, and monitoring systems required by conventional therapeutic interventions.
Solution Approach 2:
Instead of using complex drugs that block aggregation pathways, the invention uses sDSS1 as a simple intermediary protein that directly binds to pathogenic proteins, simplifying the therapeutic approach while maintaining high efficacy in preventing protein aggregation.
3Ease of operation
If the organism relies on natural protein removal mechanisms, then no external intervention is needed, but the removal capacity is insufficient during aging and disease states
Solution Approach 1:
The sDSS1 protein serves as an external intermediary agent that supplements the organism's natural protein removal mechanisms. It can be administered externally and works within the body to enhance junk protein clearance, combining the simplicity of natural mechanisms with the enhanced capacity of external intervention.
Solution Approach 2:
The sDSS1 protein provides universal protection against multiple types of junk proteins including oxidized proteins, glycated proteins, and amyloid proteins. This multi-functionality allows a single external intervention to address various protein accumulation diseases without requiring different treatments for each condition.
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 sDSS1 protein effectively shields cells from cytotoxicity induced by oxidized, glycosylated, and amyloid proteins, demonstrating potential as a therapeutic agent for diseases related to excessive protein accumulation by reducing protein aggregation and promoting cell viability.
Implementation Method 1
the sDSS1 protein, as a highly conservative small protein in eukaryote, can be covalently modified to oxidized protein under the conditions of enzymatic reaction and ATP consumption
Implementation Method 2
forming conjugates with oxidized and amyloid proteins without energy-consuming enzymatic reactions, thereby reducing their cytotoxicity
Data Source
AI summary
The disclosure of the present application relates to a secretory deleted split hand/split foot 1 (sDSS1) protein, the amino acid sequence thereof, the nucleic acid sequence thereof, and the applications of the same. The sDSS1 protein is a secretory protein from higher primate, and can be detected in human serum and cerebral spinal fluid (CSF). The sDSS1 protein can form conjugate with oxidized protein under nonenzymatic condition or with amyloid-beta (Aβ) polypeptide to reduce formation of Aβ oligomer. The addition of sDSS1 protein to culture medium can shield the cytotoxicity induced by oxidized protein, Aβ oligomer, amylin oligomer and glycosylated protein, so as to protect the cells against these toxoproteins. The sDSS1 protein can prolong survival time of senescence-accelerated mice significantly. The protein can be used to prevent and treat the diseases induced by oxidized protein, glycated protein, Aβ protein accumulation, amylin protein accumulation or excessive formation or accumulation of other pathogenic proteins with similar features, and has important potential in biological medicine.