Surface Modified Proteinaceous Spherical Particles for Amyloid Binding
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Solution Overview
Problem
Current treatments and diagnostic methods are ineffective in preventing the formation and aggregation of amyloid plaques, particularly those caused by Amyloid Beta (Aβ), which are associated with diseases like Alzheimer's, and lack effective means for systemic reduction and detection of these plaques.
Innovation Solution
Surface modified proteinaceous particles (SMOPs) with an amyloid-binding moiety, such as KLVFF, are created through sonication, forming a protein layer with disulfide bonds, which bind to Aβ, preventing aggregation and toxicity, and can be used for both therapeutic and diagnostic purposes by migrating to amyloid plaque sites and being detected using contrasting agents.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If current treatments and diagnostic methods are used, then existing therapeutic approaches are applied, but they are ineffective in preventing formation and aggregation of amyloid plaques
Solution Approach 1:
The patent introduces SMOPs as an intermediary agent that mediates between the body's immune system and amyloid plaques. The particles bind to Aβ through amyloid-binding moieties and are recognized by phagocytic cells, facilitating clearance without requiring direct intervention in the complex amyloid aggregation pathway.
Solution Approach 2:
The invention changes the physical and chemical parameters of the therapeutic agent by using proteinaceous particles with specific surface modifications. The particles are engineered with controlled size (micrometer scale), surface charge, and binding affinity to optimize both stability in circulation and recognition by immune cells.
2Difficulty of detecting and measuring
If diagnostic methods are used to detect amyloid plaques, then detection capability is provided, but current methods lack effective means for systemic detection
Solution Approach 1:
The SMOPs are designed with multi-functionality, serving both therapeutic and diagnostic purposes. The same particle that binds and clears Aβ can also be detected by imaging modalities when equipped with appropriate contrast agents, eliminating the need for separate diagnostic agents.
Solution Approach 2:
The patent employs contrasting agents that enable detection through various imaging modalities. These agents may include radioactive isotopes for PET/SPECT imaging, magnetic particles for MRI, or fluorescent dyes, allowing the particles to be tracked systemically and visually detected in regions of high amyloid burden.
3Reliability
If amyloid-binding moieties are added to protein particles, then binding to Aβ is achieved, but complexity of particle structure increases
Solution Approach 1:
The SMOP structure is segmented into distinct functional modules: a proteinaceous core providing structural stability and biocompatibility, surface-bound amyloid-binding moieties for specific Aβ recognition, and optional contrasting agents for detection. This modular architecture simplifies the design and manufacturing process while maintaining high binding affinity.
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
SMOPs effectively reduce Aβ concentration and aggregation, mitigate toxicity, and facilitate diagnostic detection of amyloid plaques, offering a novel approach to treating and diagnosing amyloid-mediated diseases by forming complexes that are recognized and cleared by cells.
Implementation Method 1
the amyloid-binding moiety on the surface of the SMOP binds to an amyloid forming protein, such as Aβ (both soluble and aggregated forms) to form an SMOP-Aβ complex
Implementation Method 2
a protein having a thiol group, for example, a cysteine residue, is combined with a biologically active agent having a thiol group to form a mixture, and the mixture is sonicated to form SMOPs
Implementation Method 3
the protein layer is spherical in shape and comprises proteins linked to each other by disulfide bonds
Implementation Method 4
the SMOP-Aβ is then recognized by cells (including macrophages) which perform phagocytosis, thereby eliminating the SMOP-Aβ complex
Data Source
AI summary
An aspect of embodiments of the invention relates to surface modified proteinaceous spherical particles (SMOP). SMOPs according to an embodiment of the invention may comprise a protein layer and an amyloid-binding moiety bound to the protein. In an embodiment, the protein layer is spherical in shape and comprises proteins linked to each other by disulfide bonds. It is suggested that SMOPs are effective in preventing formation of amyloid and aggregation of Aβ when administered to a patient in need thereof.