Science
Mechanism of Action
This single-chain recombinant human peptide, produced in E. coli using a human aquaporin-1 (AQP-1) gene, is crucial for epidermal water homeostasis. Aquaporins create permeable channels in cell membranes, enabling water passage. As skin hydration naturally declines with age due to reduced aquaporin levels, RH-POLYPEPTIDE-64 intervenes by stimulating Filaggrin synthesis. Filaggrin is vital for the skin’s internal moisture system, breaking down into free amino acids that form key components of the natural moisturizing factor (NMF), which actively captures water and minimizes transepidermal water loss. Furthermore, AQP-1 is involved in water exchange between the blood and dermis, supports cellular response to hypertonic stress, and increases hydraulic pressure, collectively improving cell migration and skin renewal. Peptides generally also signal the body’s intrinsic skin repair mechanisms.
Research
Clinical Evidence
Low confidenceN/A
Transparency
Dusting Analysis
The Formula
Formulation
Stability
While specific optimal pH for RH-POLYPEPTIDE-64 is not detailed, peptides are generally pH-sensitive. Other polypeptides show stable hydrodynamic diameters within ranges such as pH 3.5-10.8 or 4.5-11. Maintaining protein integrity and protection from pH extremes is critical for formulation stability.
Safety
Safety Profile
Specific safety assessments by CIR, SCCS, or FDA for RH-POLYPEPTIDE-64 are currently unavailable. However, as a recombinant human peptide, it belongs to an ingredient class generally considered within cosmetic safety evaluations.
Your Skin
Skin Compatibility
Our Assessment
Verdict
RH-POLYPEPTIDE-64 is a valuable ingredient for comprehensive skin hydration, barrier reinforcement, and cellular renewal due to its unique mechanism involving aquaporin-1 and natural moisturizing factor synthesis.
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References
Sources