Monovalent Antibodies Targeting Galectin-7 Dimerization
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Solution Overview
Problem
Current galectin inhibitors for cancer treatment are limited by a lack of specificity and high affinity, particularly for galectin-7, due to structural homology in glycan binding sites and limited understanding of less-well-known galectins, leading to ineffective cancer immunotherapy.
Innovation Solution
Development of monovalent antibodies specifically targeting human galectin-7 (hGAL-7) dimerization with defined complementarity determining regions (CDRs) to inhibit hGAL-7 activity and dimerization, potentially disrupting its immunosuppressive functions in cancer cells.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If conventional galectin inhibitors are used, then broad galectin family inhibition is achieved, but specificity for galectin-7 is lost due to structural homology in glycan binding sites
Solution Approach 1:
The patent develops monovalent antibodies with specifically engineered CDR regions that target unique local structural features of galectin-7's carbohydrate recognition domain, rather than the conserved glycan binding site. This local quality approach allows differentiation between structurally similar galectins by focusing on variable regions specific to GAL-7
Solution Approach 2:
The invention segments the antibody structure into monovalent units with defined CDR combinations, each targeting specific epitopes on galectin-7. This segmentation enables precise control over binding specificity and affinity, allowing the antibody to distinguish galectin-7 from other galectin family members despite their structural homology
2Strength
If multivalent antibodies are used to increase affinity, then binding strength is improved, but dimerization interference capability is reduced
Solution Approach 1:
Instead of using multivalent antibodies that bind to separate epitopes, the patent inverts the approach by designing monovalent antibodies that specifically bind to the dimerization interface epitope. This single valency design allows the antibody to physically block dimer formation while maintaining sufficient binding affinity through optimized CDR interactions with the interface region
3Adaptability or versatility
If polyclonal antibodies are used, then broad recognition is achieved, but precision in targeting galectin-7 dimerization interface is reduced
Solution Approach 1:
The patent creates highly precise copies of the ideal antibody binding site through engineered CDR sequences that are optimized for specific epitope recognition. Rather than relying on the heterogeneous mixture of polyclonal antibodies, the invention uses precisely copied and optimized CDR regions that maintain high specificity for the galectin-7 dimerization interface
Data Source
AI summary
Monovalent antibodies such as nanobodies that are specific for galectin-7 are described. These monovalent antibodies are able to interfere with the dimerization of galectin-7, and thus may be used for the treatment of diseases associated with dysregulated galectin-7 expression and/or activity, such as certain types of cancers as well as eye diseases or conditions associated with pathological neovascularization or angiogenesis.