FITAKH Recombinant Collagen Type I + Type III: Innovative Chimeric Dual‑Collagen Composite Structure

In the market, single-component collagen has obvious application shortcomings: Type Ⅰ collagen only focuses on skin support with weak moisturizing and repairing capacity; Type Ⅲ collagen mainly soothes and softens skin without sufficient supporting effect.

FITAKH Recombinant Type Ⅰ+Ⅲ Collagen Lyophilized Powder (Master Document Filing No. M2026235-000) adopts an innovative chimeric dual-collagen composite structure. Its complete mechanism, cellular activity, in-vivo and human trials are verified by authoritative SCI literatures, and all test data are fully archived in the master document.

Collagen accounts for over 70% of human dermis dry weight. Type Ⅰ and Type Ⅲ collagen interweave to form the native skin fiber network. Human collagen depletes at an annual rate of 1%. Repair-focused Type Ⅲ collagen is consumed much faster than supporting Type Ⅰ collagen. Unbalanced collagen ratio will trigger dryness, redness, fragile barrier, fine lines, sagging, dull and rough skin and other signs related to skin aging.

Traditional animal-extracted collagen and short-segment human-like collagen generally have drawbacks including sensitization risks, poor dermal penetration and insufficient biological activity. This lyophilized powder under Master Document Filing No. M2026235 adopts patented translational pause gene technology (Optimized gene fermentation technology to fully retain active fragments of Type I & III collagen, with much higher fermentation yield and protein activity than ordinary recombinant processes). It integrates core functional fragments of two collagens to build dual pathways of "external collagen supplementation + endogenous autologous collagen activation", realizing skin firming and barrier stabilization simultaneously.

Based on mature bioengineering R&D system, we selectively intercept cell adhesion domain of Type Ⅰ collagen and proliferation & migration domain of Type Ⅲ collagen, equipped with cysteine-rich C-propeptide to assist collagen folding into complete triple-helix active structure (Standard spatial conformation of human native collagen, the core foundation for collagen to exert repairing and regeneration-promoting effects).

Synonymous codon optimization (Adjust gene expression sequence to reduce protein folding loss and greatly improve activity retention of lyophilized powder finished products) is adopted to build translational pause sites, achieving prokaryotic aseptic fermentation yield of 1.36g/L with biological activity far exceeding common recombinant collagen sold on the market.

After multiple aseptic purification, the stock solution is processed by low-temperature vacuum freeze-drying to inhibit oxidative deactivation and realize long-term stable storage at room temperature. The finished product contains no heterologous protein or residual chemical crosslinking agent, with Grade 0 cytotoxicity, suitable for all skin types and all post-aesthetic repair scenarios.

Basic Supply Parameters Table