Nucleic Aptamers for Factor H Purification
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Solution Overview
Problem
Current methods for purifying Factor H from blood plasma are either costly due to excessive heparin consumption or do not achieve sufficient purity for therapeutic use.
Innovation Solution
Development of nucleic aptamers that selectively bind to Factor H, allowing for its purification through affinity chromatography, reducing heparin usage and enhancing purity levels.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Manufacturing precision
If heparin-type affinity chromatography is used to purify Factor H, then purification effectiveness is improved, but cost increases due to excessive heparin consumption
Solution Approach 1:
The patent replaces expensive heparin with a cost-effective recombinant protein ligand (Fc fusion protein or albumin fusion protein) that can be produced in large quantities through recombinant DNA technology. This disposable ligand approach eliminates the need for costly heparin while maintaining purification effectiveness.
Solution Approach 2:
The patent changes the chemical and structural parameters of the affinity ligand from heparin (a polysaccharide) to recombinant proteins with specific domains (Fc region or albumin variants). This parameter change allows for controlled expression, purification, and reuse of the ligand, reducing overall consumption costs.
2Manufacturing precision
If conventional purification processes are used, then some purification is achieved, but purity level remains insufficient for therapeutic use
Solution Approach 1:
The patent extracts and isolates specific domains from heparin-binding proteins (Fc region of antibodies or albumin variants) that retain high affinity for Factor H. By taking out only the essential binding domains and fusing them to stable protein backbones, the patent creates highly specific affinity ligands that achieve therapeutic-grade purity.
Solution Approach 2:
The patent creates composite affinity ligands by fusing heparin-binding domains (Fc or albumin) with purification tags or stabilizing structures. These composite proteins combine the high affinity of natural heparin-binding regions with the stability and ease of production of recombinant proteins, achieving both high purity and therapeutic suitability.
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 use of nucleic aptamers enables efficient and cost-effective purification of Factor H, achieving high purity suitable for therapeutic applications while minimizing heparin consumption.
Implementation Method 1
nucleic aptamers that selectively bind to Factor H, allowing for its purification through affinity chromatography
Data Source
Figure 1A~1B
Figure 2A
Figure 2B
AI summary
The invention relates to nucleic acid aptamers binding specifically to factor H, to a method for obtaining same, and to the uses thereof, in particular for the purposes of purifying factor H.