Tetrapeptide Sequences for Dermal Extracellular Matrix Protein Upregulation
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Solution Overview
Problem
Current cosmetic peptides fail to effectively upregulate dermal extracellular matrix proteins such as fibrillin, fibronectin, decorin, collagen I, and collagen IV, which are crucial for skin integrity and repair, leading to inadequate skin regeneration and anti-aging benefits.
Innovation Solution
Development of tetrapeptides with specific amino acid sequences, such as U-XXGD-Z, where X denotes Glutamic acid, Lysine, Leucine, Alanine, or Arginine, and modifications at the N-terminal and C-terminal ends, which act as signaling matrikines to enhance the production of these proteins.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If conventional cosmetic peptides are used, then skin repair and regeneration are stimulated, but the upregulation of dermal extracellular matrix proteins (fibrillin, fibronectin, decorin, collagen I, collagen IV) is insufficient
Solution Approach 1:
The patent modifies the amino acid sequence parameters of the peptide by incorporating specific residues (Proline at position 2, Glutamic acid at position 3, Aspartic acid at position 4) and adjusting N-terminal modifications (palmitoyl, myristoyl, biotinyl groups) to optimize binding affinity and signaling capability for dermal extracellular matrix protein upregulation
Solution Approach 2:
The invention creates a composite peptide structure combining multiple functional elements: N-terminal fatty acid modifications (palmitoyl, myristoyl, or biotinyl groups), a core tetrapeptide sequence (Pro-Glu-Asp-Xaa), and C-terminal modifications, where each component contributes specific biological activities to achieve synergistic effects on skin repair and ECM protein production
2Quantity of substance
If peptide sequences are modified to enhance protein upregulation, then dermal extracellular matrix protein production increases, but peptide synthesis complexity increases
Solution Approach 1:
The patent divides the peptide into distinct functional segments: N-terminal modification group (palmitoyl, myristoyl, or biotinyl), core tetrapeptide sequence (Pro-Glu-Asp-Xaa where Xaa is a specific amino acid), and C-terminal group (OH, NH2, or NH-R), allowing for modular design and systematic optimization of each segment's contribution to protein upregulation
Solution Approach 2:
The invention systematically varies specific parameters within the peptide structure, particularly the N-terminal modification type and the C-terminal amino acid residue, to optimize the balance between synthesis feasibility and biological activity for dermal extracellular matrix protein production
Data Source
AI summary
According to the present invention, there is provided a tetrapeptide, capable of inducing dermal extracellular matrix protein upregulation, having the amino acid sequence U-(SEQ ID No: 1)-Z, U-(SEQ ID No: 2)-Z, U-(SEQ ID No: 3)-Z, U-(SEQ ID No: 4)-Z, U-(SEQ ID No: 5)-Z, U-(SEQ ID No: 6)-Z, U-(SEQ ID No: 7)-Z, U-(SEQ ID No: 8)-Z, U-(SEQ ID No: 9)-Z, U-(SEQ ID No: 11)-Z, U-(SEQ ID No: 12)-Z, U-(SEQ ID No: 13)-Z, U-(SEQ ID No: 14)-Z, U-(SEQ ID No: 15)-Z, U-(SEQ ID No: 16)-Z, U-(SEQ ID No: 17)-Z, U-(SEQ ID No: 18)-Z, U-(SEQ ID No: 19)-Z, U-(SEQ ID No: 20)-Z, U-(SEQ ID No: 21)-Z, U-(SEQ ID No: 22)-Z, U-(SEQ ID No: 23)-Z, U-(SEQ ID No: 24)-Z, U-(SEQ ID No: 25)-Z, U-(SEQ ID No: 26)-Z, U-(SEQ ID No: 27)-Z, U-(SEQ ID No: 28)-Z, and U-(SEQ ID No: 29)-Z.