Collagen, the fourth most abundant protein found in the body, is the principal structural protein found in the body’s molecular scaffolding. The scaffolding is a complex matrix of proteins and proteoglycans that support the internal organs as well as the skin.
Collagen itself, like all proteins, is a heteropolymer composed of more than 1400 amino acid residues linked via peptide bonds. What distinguishes collagen is the degree to which those amino acid residues are conserved. Every third residues is a glycine molecule. Most typically the glycine is then followed by proline and hydroxyproline. In fact it is the presence of the proline that contributes to collagen’s dense structure. Hydroxyproline, formed by the oxidation of proline in the presence of Vitamin C, stabilizes the collagen helix.
Many researchers over the years have determined that breaking down collagen with either alkaline, or enzymatic hydrolysis produces a product that can increase the collagen production of cultured cells three-fold.
Alkaline and to a lesser extent enzymatic hydrolysis produce random peptide fragments which cannot be relied upon to produce consistent results in cell culture models. Further biochemical research has revealed that the sequence Glycine-Proline-Hydroxyproline (G-P-Hyp) is the active present in collagen hydrolysates.
Having determined the active principal, two hurdles remained: delivery and economics. Traditional collagen hydrolysates have a molecular weight greater than 1000 Daltons (D) and as such are not capable of readily penetrating the skin. While it is possible to hydrolyze the protein reducing the molecular weight to less than 300 D, which would allow penetration, it is not possible to do so while producing a product of adequate purity. Advances in peptide synthesis centered on a new base labile amino-protective group overcome the question of purity and have made feasible the economic commercial production of pure peptides.
FSS Collagen Prepeptide PF is pure (>99.7%) G-P-Hyp tripeptide produced synthetically, without the use of animal derived products or genetically modified organisms. With a molecular weight of 285 D it shows excellent bioavailability. In-vitro experiments have shown that this material will dramatically increase synthesis of Collagen.