Aggrelyte Composition for Solubilizing Aggregated Lens Proteins
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Solution Overview
Problem
Presbyopia, a vision-impeding condition affecting millions due to lens stiffening from age-related protein crosslinking and aggregation, lacks effective compositions and methods for prevention, delay, or reversal.
Innovation Solution
Administration of aggrelytes, such as N,S-diacetyl-L-cysteine methyl ester, S-acetyl-N-(3,3-dimethylbutanoyl)-L-cysteinate, and N-acetyl cysteine methyl ester, to solubilize aggregated lens proteins and reduce lens stiffness by acetylation and breaking disulfide bonds.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Stability of the object's composition
If lens proteins undergo posttranslational modifications and crosslinking over time, then lens structural stability is improved, but lens flexibility and accommodation ability deteriorate
Solution Approach 1:
The patent applies parameter changes by modifying the chemical state of lens proteins through acetylation. Specifically, aggrelytes convert aggregated, crosslinked lens proteins into acetylated forms that are more soluble and flexible. This chemical parameter transformation reverses the age-related stiffening while preserving structural integrity, thereby restoring accommodation ability without compromising lens stability.
Solution Approach 2:
The patent converts the harmful effect of protein aggregation and crosslinking into a beneficial outcome. By administering aggrelytes, the aggregated proteins that cause stiffness are transformed into acetylated proteins that regain solubility and flexibility. The same proteins that originally caused presbyopia are repurposed to restore lens function through controlled chemical modification.
2Duration of action of stationary object
If lens proteins accumulate and crosslink with age, then lens durability is improved, but lens solubility and protein turnover deteriorate
Solution Approach 1:
The patent changes the chemical parameters of lens proteins by introducing acetylation modifications. This parameter change transforms insoluble, crosslinked proteins into soluble, acetylated proteins that can be processed and turned over normally. The durability of the lens is maintained while protein solubility and turnover are restored through this chemical transformation.
3Strength
If disulfide bonds form in lens proteins, then lens structural integrity is improved, but lens flexibility and accommodation deteriorate
Solution Approach 1:
The patent applies parameter changes by chemically modifying disulfide bonds through reduction and subsequent acetylation. This transformation alters the bond characteristics from rigid disulfide linkages to more flexible acetylated structures, thereby restoring lens flexibility and accommodation ability while preserving essential structural integrity.
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
Aggrelytes effectively solubilize aggregated lens proteins, reduce lens stiffness, and acetylate lysine residues, potentially reversing or delaying presbyopia symptoms without toxicity to lens epithelial cells or corneas.
Implementation Method 1
acetylation of lens proteins and reduction of disulfide bonds in lens proteins
Implementation Method 2
reduction of disulfide bonds in lens proteins
Data Source
AI summary
Methods of treating, preventing, delaying, or reversing presbyopia in a subject involve administering a pharmaceutically effective amount of an aggrelyte to the subject. The aggrelyte may be one or more of N,S-diacetyl-L-cysteine methyl ester, S-acetyl-N-(3,3,-dimethylbutanoyl)-L-cysteinate, or N-acetyl cysteine methyl ester. The aggrelyte may be administered topically.