Humanized Anti-MUC5AC Radiolabeled Antibody for Tumor Accumulation
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Solution Overview
Problem
Existing antibodies for mucin subtype 5AC (MUC5AC) lack specificity and effective tumor accumulation, limiting their effectiveness in diagnostic and therapeutic applications.
Innovation Solution
A conjugate of a chelating agent chelated with a radionuclide and a humanized antibody specifically binding to MUC5AC is developed, utilizing specific amino acid sequences for enhanced specificity and tumor accumulation.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Measurement precision
If existing antibodies are used for MUC5AC detection, then basic detection function is achieved, but specificity and tumor accumulation are insufficient
Solution Approach 1:
The patent applies parameter changes by modifying the antibody structure through humanization techniques, changing the amino acid sequences to achieve both high specificity for MUC5AC and improved tumor accumulation. The humanized antibody maintains the original antibody's binding specificity while improving its pharmacokinetic properties and reducing immunogenicity, thereby simultaneously achieving measurement precision and reliability.
2Measurement precision
If mouse antibody is used, then MUC5AC binding is achieved, but immunogenicity and specificity in human patients are limited
Solution Approach 1:
The patent transforms the mouse antibody into a humanized antibody by changing the amino acid sequence parameters. This involves replacing mouse-specific amino acid sequences with human-like sequences while preserving the complementarity-determining regions (CDRs) that provide MUC5AC binding specificity. This parameter change reduces immunogenicity in human patients while maintaining binding precision.
Solution Approach 2:
The humanized antibody represents a composite structure combining mouse CDR regions for antigen recognition with human framework regions for reduced immunogenicity. This composite approach allows the antibody to maintain its original binding specificity while being more compatible with the human immune system.
3Reliability
If chimeric antibody is used, then improved tumor targeting is achieved, but manufacturing complexity increases
Solution Approach 1:
The patent simplifies the antibody structure by progressing from chimeric to fully humanized design. This parameter change in the degree of humanization reduces manufacturing complexity while maintaining or improving tumor accumulation through optimized amino acid sequences and reduced immunogenicity.
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 conjugate demonstrates superior specificity for MUC5AC and increased tumor accumulation, improving diagnostic imaging and therapeutic efficacy.
Implementation Method 1
the radionuclide is a metal nuclide that emits α particle or positron
Implementation Method 2
a conjugate of a chelating agent chelated with a radionuclide
Data Source
AI summary
The RI-labeled anti-MUC5AC humanized antibody of the present invention is a conjugate of a chelating agent chelated with a radionuclide and an antibody (the radionuclide is a metal nuclide that emits α particle or positron, and the antibody is a humanized antibody specifically binding to MUC5AC), and is superior in specificity for MUC5AC and accumulation in tumor. Therefore, it is extremely useful for the treatment and/or diagnosis of diseases in which MUC5AC is overexpressed, particularly cancer.