Monoclonal Antibody for Specific D-dimer Detection
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Solution Overview
Problem
Current diagnostic agents for detecting D-dimer and cross-linked fibrin have low specificity and often misdiagnose due to recognition of low-molecular weight fibrin degradation products rather than fully digested D-dimer, especially in patients with disseminated intravascular coagulation and those under anticoagulation treatment.
Innovation Solution
A murine monoclonal antibody specifically reacting to D-dimer and its derivatives, recognizing the N-terminal amino acid sequence 134 to 142 of the beta-chain and 124 to 214 of the alpha-chain, is developed, which is used in a diagnostic agent that includes a primary antibody and a secondary antibody conjugated with a marker for quantitative detection via ELISA or similar methods.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If conventional diagnostic agents are used to detect D-dimer, then detection can be performed, but specificity is low and misdiagnosis occurs due to recognition of low-molecular weight fibrin degradation products
Solution Approach 1:
The monoclonal antibody is designed to recognize a specific local epitope (amino acids 134-142 of the beta-chain and 124-214 of the alpha-chain) on the D-dimer molecule. This localized recognition ensures high specificity for fully degraded D-dimer while avoiding cross-reactivity with partially degraded fibrin products that lack this specific epitope configuration.
Solution Approach 2:
The invention changes the molecular weight parameter by specifically targeting fully degraded D-dimer (lower molecular weight) versus partially degraded cross-linked fibrin (higher molecular weight). The antibody's binding specificity is tuned to recognize only the fully degraded form, thereby improving diagnostic precision by excluding false positives from intermediate degradation products.
2Measurement precision
If monoclonal antibodies recognizing low molecular weight fibrin degradation products are used, then detection sensitivity increases, but false positive results occur in patients with disseminated intravascular coagulation and anticoagulation treatment
Solution Approach 1:
The invention converts the potential harm of cross-reactivity into a benefit by designing the antibody to specifically recognize the epitope that is only present in fully degraded D-dimer. The antibody's strict specificity for amino acids 134-142 of beta-chain and 124-214 of alpha-chain acts as a filter that excludes partially degraded products, thereby eliminating false positives while maintaining detection of true D-dimer.
3Adaptability or versatility
If different monoclonal antibodies are used in various diagnostic agents, then multiple detection methods are available, but test results show significant differences due to recognition of different cross-linked fibrin degradation products
Solution Approach 1:
The monoclonal antibody is designed with universal applicability for detecting all forms of fully degraded D-dimer regardless of the source or method of degradation. By targeting a conserved epitope region (amino acids 134-142 of beta-chain and 124-214 of alpha-chain), the antibody ensures consistent results across different diagnostic applications and patient conditions, establishing a universal standard for D-dimer detection.
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 monoclonal antibody provides high specificity and accurate quantification of D-dimer and cross-linked fibrin derivatives, improving diagnostic accuracy by distinguishing between fully degraded and partially degraded fibrin, thus enhancing the detection of D-dimer levels in plasma.
Implementation Method 1
a murine monoclonal antibody specifically reacting to D-dimer and its derivatives, recognizing the N-terminal amino acid sequence 134 to 142 of the beta-chain and 124 to 214 of the alpha-chain
Data Source
AI summary
Disclosed are a monoclonal antibody against human D-dimer produced in a mouse and high molecular weight cross-linked fibrin including a corresponding epitope, a cell line secreting the monoclonal antibody, and methods for producing the same. The anti-D-dimer monoclonal antibody of the present invention may be effectively used as a diagnotic agent for screening and detecting in-vivo D-dimer, and high molecular weight cross-linked fibrin and its derivatives containing the D-dimer since the monoclonal antibody specifically reacts with D-dimer, and cross-linked fibrin and its derivatives containing the D-dimer, which do not bind to human fibrinogen or fibrin.