Recombinant Antibody CDR Sequences for cTnI Detection
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Solution Overview
Problem
Existing antibodies for detecting cardiac troponin I (cTnI) have low activity and poor affinity, making them ineffective for sensitive and specific detection of cTnI protein.
Innovation Solution
A novel isolated binding protein with a high affinity for human cTnI protein is developed, comprising specific antigen-binding domains with complementarity determining regions (CDRs) that exhibit strong binding activity.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Measurement precision
If existing antibodies are used for detecting cTnI, then the detection method can be implemented, but the activity and affinity are low resulting in poor detection sensitivity and specificity
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequences of the complementarity determining regions (CDRs) in the antibody variable regions. Specifically, the patent defines specific CDR sequences (CDR-VH1, CDR-VH2, CDR-VH3, CDR-VL1, CDR-VL2, CDR-VL3) with particular amino acid compositions that optimize binding affinity and specificity for cTnI, thereby improving detection sensitivity and reliability
Solution Approach 2:
The patent creates a composite antibody structure by combining specifically designed variable regions (containing optimized CDRs) with constant regions (IgG1, IgG2, IgG3, or IgG4). This composite construction integrates the high-affinity binding capability of the engineered variable regions with the functional properties of the constant regions, resulting in an antibody with superior detection performance
2Reliability
If existing antibodies are used, then the detection system can be established, but the affinity for cTnI is poor making effective and specific detection difficult
Solution Approach 1:
The patent improves binding affinity by changing the physical-chemical parameters of the antibody through specific amino acid sequences in the CDR regions. The defined sequences (e.g., CDR-VH1: G-F-N-X1-K-X2-Y-X3-M-H with specific constraints on X1, X2, X3) are designed to maximize complementary interactions with the cTnI antigen, thereby enhancing binding strength and detection precision
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 binding protein demonstrates high sensitivity and specificity in detecting cTnI, enabling effective diagnosis of acute myocardial infarction and other cardiomyocyte damage-related conditions.
Implementation Method 1
the antigen-binding domain comprises at least one complementarity determining region, which has an amino acid sequence as follows; or which has at least 80% sequence identity to the complementarity determining region having the amino acid sequence as follows and has an affinity for the cardiac troponin I at a KD value that is less than or equal to 1.41×10−9 mol/L
Data Source
AI summary
The present invention provides an isolated binding protein comprising a cTnI antigen binding domain. The antigen binding domain comprises at least one complementarity determining region selected from amino acid sequences defined herein, or has sequence identity of at least 80% to the complementarity determining region of said amino acid sequence and an affinity of KD≤1.41×10−9 mol/L to cTnI. The binding protein can be used for detection of cTnI protein.