Tetrapeptide Sequences for Dermal ECM Protein Upregulation
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Solution Overview
Problem
Current cosmetic peptides, such as Pal-KKTKS and Pal-GQPR, while effective, do not fully address the need for new biologically active peptides to support skin's natural behaviors and upregulate dermal extracellular matrix proteins like fibrillin, fibronectin, and collagen I effectively.
Innovation Solution
Development of tetrapeptides with specific amino acid sequences, such as U-LSXX-Z, where L is Leucine and S is Serine, and X can be Valine, Aspartic acid, Proline, or Glycine, designed to upregulate dermal extracellular matrix proteins by acting as signaling matrikines, with modifications at the N-terminal and C-terminal ends to enhance bioavailability.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If existing peptide matrikines (Pal-KKTKS, Pal-GHK, Pal-GQPR) are used in cosmetic compositions, then skin repair and regeneration are stimulated, but the ability to effectively upregulate dermal extracellular matrix proteins (collagen I, fibrillin, fibronectin) is insufficient
Solution Approach 1:
The patent modifies the amino acid sequence parameters of existing peptide matrikines by substituting specific residues (e.g., changing Pal-GHK to Pal-LSDV, Pal-LSPG, or Pal-LSVD) to create novel tetrapeptides with enhanced ability to upregulate dermal ECM proteins while maintaining skin repair and regeneration activities
Solution Approach 2:
The patent combines multiple tetrapeptide variants (Pal-LSDV, Pal-LSPG, Pal-LSVD) in specific compositions to achieve synergistic effects that enhance both skin repair capabilities and ECM protein upregulation beyond what single peptides can accomplish
2Ease of operation
If peptide sequences are modified to enhance bioavailability (adding N-terminal modifications and C-terminal modifications), then skin penetration and activity are improved, but the complexity of peptide synthesis and formulation increases
Solution Approach 1:
The patent incorporates N-terminal modifications (such as palmitoyl groups) and C-terminal modifications (such as amide or acid groups) directly into the synthesized peptide structure during manufacturing, ensuring optimal bioavailability and skin penetration characteristics are built-in from the outset rather than requiring post-synthesis modifications
Solution Approach 2:
The patent systematically varies the N-terminal and C-terminal functional groups across different tetrapeptide variants to optimize the balance between bioavailability enhancement and synthesis feasibility, selecting modifications that provide sufficient skin penetration improvement without excessive formulation complexity
Data Source
AI summary
According to the present invention, there is provided a tetrapeptide, capable of inducing dermal extracellular matrix protein upregulation, selected from the group consisting of tetrapeptides having the amino acid sequence U-LSXX-Z wherein L is used to denote amino acid Leucine and S is used to denote Serine, as per the internationally recognised single letter code for amino acids, X denotes an amino acid selected from the group consisting of Valine (V), Aspartic acid (D), Proline (P), Glycine (G) and mixtures thereof, at the N-terminal end, U is selected from the group consisting of H, —CO—R1, —SO2—R1 or a biotinyl group, at the C-terminal end, Z is selected from the group consisting of OH, O R1, NHR1 or NR1R2; wherein if U is H then Z cannot be OH and R1 and R2 are independently selected from the group consisting of alkyl, aryl, aralkyl, alkylaryl, alkoxy, saccharide and aryloxy group, which may be linear, branched, cyclical, polycyclic, unsaturated, hydroxylates, carbonylated, phosphorylated and/or sulphurous, said groups comprising from 1 to 24 carbon atoms and being capable of including one or more heteroatoms O, S and/or N.