Mutant EGF Proteins with Enhanced Thermal Stability
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Solution Overview
Problem
Conventional epidermal growth factor (EGF) proteins are sensitive to high temperatures and aqueous solutions, leading to reduced activity and limited stability, making them unsuitable for cosmetic applications where stability and activity maintenance are crucial.
Innovation Solution
Development of mutant EGF proteins with increased thermal stability and solubility by substituting hydrophobic residues with hydrophilic residues and introducing disulfide bonds, specifically through mutations such as replacing leucine with serine, isoleucine with cysteine, and aspartic acid with cysteine, to enhance stability without altering protein size.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Stability of the object's composition
If conventional EGF is used, then biological activity is achieved, but thermal stability is poor
Solution Approach 1:
The patent applies parameter changes by systematically substituting specific amino acid residues at defined positions in the EGF sequence with alternative residues having different properties. This modifies the protein's thermal stability parameter while preserving its biological activity, resolving the contradiction between stability and reliability.
Solution Approach 2:
The invention applies local quality by making targeted substitutions at specific positions (e.g., positions 3, 6, 11, 14, 17, 20, 23, 26, 29, 32, 35, 38, 41, 44, 47, 50) rather than throughout the entire sequence. Each substitution is designed to locally improve thermal stability while maintaining the overall structure and function of the EGF molecule.
2Stability of the object's composition
If conventional EGF is used, then biological activity is achieved, but solubility in aqueous solution is poor
Solution Approach 1:
The patent improves solubility by substituting hydrophobic amino acid residues with hydrophilic alternatives at specific positions in the EGF sequence. This parameter change in residue polarity enhances the protein's solubility in aqueous solutions while maintaining its biological activity.
3Stability of the object's composition
If EGF is stabilized for cosmetic use, then stability is improved, but production cost increases
Solution Approach 1:
The invention achieves stability improvement through rational protein design with specific amino acid substitutions, eliminating the need for complex stabilization formulations or expensive purification processes. This approach reduces production costs while maintaining high stability, making the EGF suitable for cosmetic applications.
Data Source
AI summary
There are provided mutants prepared by changing a DNA base sequence and an amino acid sequence of an epidermal growth factor (EGF), in which a mutant EGF protein has excellent thermal stability and stability even in the state of an aqueous solution, and a gene encoding the protein are provided; a recombinant vector including the gene and a microorganism transformed by the recombinant vector are provided; a method of preparing the mutant EGF protein is provided; a cosmetic composition for accelerating the growth of skin cell and skin regeneration, including the protein, the gene, or the recombinant vector, is provided; and by preparing a product using the EGF mutant according to the present invention, it is possible to produce functional cosmetics, in which the activity thereof is maintained even during a distribution and storage process unlike the conventional wild-type EGF product.