Superfolder GFP Fusion Carrier for Recombinant Peptide Production
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Solution Overview
Problem
Current methods for producing recombinant peptides face challenges such as high costs, low yields, and environmental concerns due to chemical synthesis, and existing fusion protein systems struggle with efficient expression and purification, especially for peptides shorter than 50 amino acids.
Innovation Solution
Employing superfolder green fluorescent protein or its mutants as a carrier protein to create stable expression systems for recombinant peptides, which are expressed in bacterial cells and can be easily purified, protecting against proteolytic degradation and allowing for high yields.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Adaptability or versatility
If chemical synthesis is used to produce peptides, then a variety of therapeutic peptides can be prepared, but the costs continuously ascend and multiple condensation reactions with tedious protection and purification processes are required
Solution Approach 1:
The patent uses fusion carrier proteins as intermediary vehicles to produce target peptides. The carrier protein-fusion peptide construct allows peptides to be produced through recombinant expression in host cells, avoiding the need for chemical synthesis. After production, the carrier protein can be removed through proteolytic cleavage or other methods, leaving the pure target peptide. This intermediary approach transforms the manufacturing process from complex chemical synthesis to simpler biological expression.
2Quantity of substance
If chemical synthesis is used for peptides with more than 50 amino acid residues, then the peptide can be produced, but the yields are low and excessive organic waste is generated making it economically unfavourable
Solution Approach 1:
The patent changes the fundamental parameter of peptide production from chemical synthesis to recombinant biological expression. This parameter change enables production of peptides with more than 50 amino acid residues at high yields without generating excessive organic waste, as the biological expression system uses cellular machinery to produce peptides in a more efficient and environmentally friendly manner.
3Quantity of substance
If existing fusion carrier proteins are used for peptide expression, then peptides can be produced, but the final yields typically do not exceed 100 mg/L and many technical problems exist especially for peptides smaller than 50 amino acid residues
Solution Approach 1:
The patent employs novel fusion carrier proteins with specific properties (such as temperature-sensitive instability or specific cleavage sites) that allow for easy removal after peptide production. These carrier proteins serve their purpose temporarily during expression and purification, then can be efficiently removed or degraded, enabling high-yield production of peptides while simplifying the purification process. This approach overcomes the limitations of traditional carrier proteins that remain in the final product or require complex removal steps.
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 efficient and cost-effective production of recombinant peptides with high yields, overcoming the limitations of existing methods by providing stable expression and simplified purification processes.
Implementation Method 1
employing superfolder green fluorescent protein or its mutants as a carrier protein to create stable expression systems for recombinant peptides, which are expressed in bacterial cells and can be easily purified, protecting against proteolytic degradation
Implementation Method 2
employing superfolder green fluorescent protein or its mutants as a carrier protein to create stable expression systems for recombinant peptides, which are expressed in bacterial cells and can be easily purified, protecting against proteolytic degradation and allowing for high yields
Implementation Method 3
employing superfolder green fluorescent protein or its mutants as a carrier protein to create stable expression systems for recombinant peptides, which are expressed in bacterial cells and can be easily purified
Data Source
AI summary
The present disclosure pertains to methods of producing recombinant peptides that contain between 10 and 200 amino acid residues using novel carrier proteins derived from superfolder green fluorescent protein and its mutants.