Modified EGF Protein Cell Permeability and Stability
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Solution Overview
Problem
Existing EGF proteins face challenges with low in vivo permeability and persistence, making them less effective in cosmetic and pharmaceutical applications for skin regeneration and wound healing.
Innovation Solution
A modified EGF protein with enhanced cell permeability and stability is developed, encoded by a specific amino acid sequence, produced using a method involving expression vectors and optimized culture conditions, and used in cosmetic and pharmaceutical compositions.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If existing EGF protein is used, then basic skin regeneration function is provided, but in vivo permeability and persistence are low
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of EGF protein through site-directed mutagenesis. Specifically, cysteine residues at positions 1 and 2 are replaced with serine or threonine residues, which changes the chemical properties of the protein and significantly improves its in vivo permeability and persistence without compromising its basic biological function
2Reliability
If EGF protein is used for cosmetic and pharmaceutical applications, then skin regeneration and wound healing effects are achieved, but protein stability under severe conditions is poor
Solution Approach 1:
The patent modifies the protein's amino acid sequence parameters to enhance stability. The replacement of cysteine residues with serine or threonine at specific positions reduces the protein's susceptibility to oxidation and aggregation, thereby maintaining its structural integrity and biological activity under severe conditions such as high temperature, extreme pH, and long-term storage
Solution Approach 2:
The patent creates a composite structure by introducing non-natural amino acids or modified amino acid residues into the EGF protein sequence. This composite approach combines the natural EGF framework with stabilizing modifications, resulting in a protein that maintains high stability while preserving skin regeneration and wound healing functions
3Productivity
If standard EGF production method is used, then basic protein production is achieved, but productivity and purification yield are insufficient
Solution Approach 1:
The patent introduces a fusion tag as an intermediary element during the production process. The modified EGF protein is initially produced as a fusion protein with a purification tag (such as His-tag or GST-tag), which facilitates easy purification through affinity chromatography. After purification, the tag can be removed to obtain the native modified EGF protein, thereby significantly improving both productivity and ease of manufacture
Data Source
AI summary
A modified EGF protein, a production method therefor, and a use thereof are disclosed. The modified EGF protein allows an effective delivery of EGF into the cell and exhibits an enhanced half-life span. A method for producing the modified EGF protein includes culturing conditions where host cell growth phase and protein expression phase employ different temperature conditions. A use of the modified EGF protein is also disclosed.


