Polyanionic Antibody Binding Partner for Electrophoresis
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Solution Overview
Problem
Existing electrophoresis methods face challenges in achieving baseline separation of binding partners and their complexes from other proteins in complex biological samples, such as blood serum, due to co-migration issues, especially when using modified antibodies that do not fully separate from serum proteins like albumin and immunoglobulins.
Innovation Solution
A method involving a binding partner with a specifically modified polyanionic polymer segment, which is capable of binding to target compounds and altering their electrophoretic mobility, allowing for baseline separation by electrophoresis in an alkaline environment, using a macromolecule with a segment for specific binding and a polyanionic polymer segment to modify the mobility of target compounds, thereby separating them from other proteins.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Measurement precision
If a modified antibody is used as a binding partner to alter electrophoretic mobility, then the target compound can be separated from other proteins, but the modified antibody and its complex may co-migrate with serum proteins such as albumin and immunoglobulins
Solution Approach 1:
The patent applies parameter changes by modifying the electrophoretic mobility of the binding partner through chemical modification with anhydrides (succinic, tricarboxylic, mellitic, or benzene tricarboxylic anhydride). This modification increases the negative charge of the antibody, thereby changing its electrophoretic mobility to achieve baseline separation from serum proteins at alkaline pH levels.
2Speed
If the binding partner is chemically modified with anhydride to increase negative charge, then electrophoretic mobility is altered, but the complex still migrates closely to human immunoglobulin and does not fully separate from uncomplexed immunoglobulin
Solution Approach 1:
The patent employs composite materials by combining the binding partner (antibody) with a polyanionic polymer segment having a number average molecular weight of at least 20 kD. This composite structure enhances the negative charge density and alters the electrophoretic mobility sufficiently to achieve baseline separation of the complex from serum proteins, overcoming the limitations of simple anhydride modification.
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
This approach enables effective baseline separation of target compounds from other proteins, even at alkaline pH, reducing interference and allowing for the determination of analytes in complex samples with improved resolution and reduced co-migration, using a binding partner with a polyanionic polymer segment that modifies the mobility of target compounds effectively.
Implementation Method 1
a binding partner for a target compound or group of target compounds which may be present in the sample
Implementation Method 2
separating the sample including the binding partner by electrophoresis in a channel comprising a separation medium in which the binding partner has a negative charge
Implementation Method 3
the binding partner being a macromolecule comprising (i) a segment capable of specifically binding to the target compound and (ii) a polyanionic polymer segment
Data Source
Figure 1
Figure 2~3
AI summary
The invention relates to a method for the analysis of a sample which may comprise a target compound or group of target compounds, the method comprising - mixing at least a portion of the sample with a binding partner for the target compound or group of target compounds, the binding partner being a macromolecule comprising (i) a segment capable of specifically binding to the target compound and (ii) a polyanionic polymer segment; and - separating the sample containing the binding partner by electrophoresis in a separation medium in which the binding partner has a net negative charge.