Antigen Binding Molecules Targeting GGGS Linker Sequences
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Solution Overview
Problem
Current antigen binding molecules, such as antibodies, face challenges in specifically binding to linker sequences like GGGS and GGGGS, which limits their application in detection, purification, and therapeutic uses due to non-specific binding and low affinity.
Innovation Solution
Development of isolated antigen binding molecules, including humanized antibodies and fragments, that specifically bind to GGGS and GGGGS sequences with high affinity, utilizing specific CDR regions and variable sequences to target these sequences with high specificity and binding efficiency.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If conventional antigen binding molecules are used to bind linker sequences, then binding occurs, but specificity is low and affinity is weak
Solution Approach 1:
The patent applies local quality by engineering specific CDR regions (CDR-H1, CDR-H2, CDR-H3, CDR-L1, CDR-L2, CDR-L3) with precise amino acid sequences to target the GGGS linker sequence. Each CDR region is optimized locally to recognize specific epitopes on the linker, while the rest of the antibody structure maintains standard immunoglobulin framework. This localized optimization achieves high specificity without requiring complete structural redesign of the entire molecule.
Solution Approach 2:
The patent employs parameter changes by systematically varying amino acid sequences in the CDR regions to optimize binding affinity and specificity. Multiple antibody variants are generated with different CDR sequences (e.g., different heavy chain CDR3 sequences like SEQ ID NO:25, 22, 19) to fine-tune the binding parameters. This includes adjusting chain length, charge distribution, and hydrophobicity in specific regions to achieve optimal binding to the GGGS linker sequence.
2Measurement precision
If antigen binding molecules are designed for high specificity to GGGS sequences, then detection precision improves, but manufacturing complexity increases
Solution Approach 1:
The patent segments the antigen binding molecule into distinct functional regions: variable regions (VH and VL) containing the CDRs responsible for specificity, and constant regions (CH1, CH2, CH3, CL) providing structural stability and effector functions. This segmentation allows independent optimization of each region - the variable regions can be engineered for high GGGS specificity while the constant regions maintain standard sequences for ease of production and expression in host cells.
Solution Approach 2:
The patent uses copying by generating multiple antibody variants based on a successful parent sequence. Once a CDR set is identified as having high affinity and specificity for GGGS linkers, this sequence template can be copied and produced at scale. The standardized framework regions serve as reusable templates, reducing manufacturing complexity while maintaining detection precision through the conserved high-affinity CDR sequences.
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 antigen binding molecules demonstrate high specificity and binding affinity to GGGS and GGGGS sequences, enabling effective detection, purification, and therapeutic applications by specifically targeting these sequences, thereby overcoming previous limitations.
Implementation Method 1
an isolated antigen binding molecule that specifically binds to a polypeptide comprising the amino acid sequence GGGS
Implementation Method 2
specifically binds to the sequence GGGS (SEQ ID NO: 1), GGGGS (SEQ ID NO: 46) or related sequences
Data Source
AI summary
Isolated antigen binding molecules that specifically binds to a molecule comprising an amino acid sequence selected from the group consisting of GGGS (SEQ ID NO: 1), GGGGS (SEQ ID NO: 46) and related sequences are provided. The antigen binding molecules may be used in the methods provided herein.