FSS Collagen PrePeptide PF
Paraben Free - Preservative Free
(Preserved with Leucidal Liquid)
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
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
Clear to Hazy Liquid
Storage: Protected from direct light and humidity at a temperature
of 50°-77°F (10°-25°C)
Shelf life: 12 months, properly stored, in sealed container.
product should be added to a formulation at the recommended usage rate.
1) Oesser et al., 2003
(Cell & Tissue Research , 311, 393-399) - showed in tissue culture HC
stimulate collagen synthesis and secretion of chondrocytes
with degraded collagen.
2. Blow, Nathan (2009).
"Cell culture: building a better matrix". Nature Methods 6 (8):
3. Fraser, R., D.; MacRae, T.
P. and Miller, A. (1987). "Molecular packing in type I collagen
fibrils". Journal of Molecular Biology 193 (1): 115–125.
4. Orgel, J. P.; et al.(2006). "Microfibrillar
structure of type I collagen in situ". PNAS 103 (24): 9001–9005.