To achieve the perfect concentration and protect the structure of the copper peptide, the active is shipped to you in a solution containing distilled water, glycerol, and preservatives. Please keep refrigerated until added to your cream.
Each tube (2 mL) is enough for about 4 fl oz of cream, serum, or gel. Use in your favorite cream or add to our Canvas Base Cream, European Cream, or our Sea Kelp Coral.
These peptides should not be added to products containing Vitamin C in any form (MAP, Ascorbic Acid, etc.)
Water, Glycerin, Copper Tripeptide-1, Propylene Glycol (and) Diazolidinyl Urea (and) Methylparaben (and) Propylparaben.
Copper ion (Cu++) has affinity for proteins, a property that is the basis for a traditional method to measure protein concentration. The N-terminal sequence of human albumin (Asp-Ala-His-Lys) is the site for the transport of copper ion in the bloodstream. Tight binding also occurs when histidine is in position 2, like in the naturally occurring copper (II) complex of Gly-His-Lys.*
The peptide Gly-His-Lys, bound or unbound to copper, has been used in skin care as an anti-aging active. Because of the widespread use of these formulations, I thought it would be interesting to go back to the original papers (1988-1992) that started this practice and re-evaluate the evidence.*
When added to a culture of human fibroblasts, Gly-His-Lys-copper induced a specific, concentration-dependent stimulation of collagen synthesis (Maquart et al. 1988). The concentrations studied were between picomolar and nanomolar (when moles are expressed in grams per volume, the numbers are given in parts per million). A later study (Wegrowski et al. 1992) showed a dose-dependent, biphasic stimulation of glycosaminoglycan synthesis (heparan sulfate and dermatan sulfate), in cultures of human skin fibroblasts. “Biphasic” means that the effect was stimulatory at very low concentrations, decreasing towards control levels at higher (but still pretty low) concentrations. The very low concentrations used were chosen because they were at order of magnitude similar to those measured in vivo.*
It is interesting that the studies on cell cultures (1988, 1992) dealt with experiments on the effect of copper peptide at concentrations in the order of picomolar (-10M), finding that higher concentrations (still minute, like 10-8M) were not beneficial. Moreover, at higher concentrations, copper peptide seems to promote protein breakdown (Allen 2001). For unknown reasons, clinical studies used much higher concentrations, e.g. 0.4%. Not surprisingly, copper peptide at those high concentrations did not help with healing (Bishop et al. 1992).*
(*See reference tab for scientific resources)
Maquart, Francois Xavier; Pickart, Loren; Laurent, Maryvonne; Gillery, Philippe; Monboisse, Jean Claude; Borel, Jacques Paul. (1988) Stimulation of collagen synthesis in fibroblast cultures by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-copper(2+). FEBS Lett. 238:343-6.
Wegrowski, Y, Maquart, FX; Borel, JP (1992) Stimulation of sulfated glycosaminoglycan synthesis by the tripeptide-copper complex glycyl-L-histidyl—Lysine-Cu2+ Life Sciences, 51 : 1049-1056
Bishop, JB; Phillips, LG; Mustoe, TA; VanderZee, AJ; Wiersema, L; Roach, DE; Heggers, JP; Hill Jr, DP et al (1992). "A prospective randomized evaluator-blinded trial of two potential wound healing agents for the treatment of venous stasis ulcers". J Vasc Surg 16 (2): 251–257
Allen, G. (2001) Specific protein degradation by copper(II) ions. In: Probing of proteins by metal ions and their low molecular weight complexes. Book Series: Metal ions in Biological systems. Volume: 38, pp. 197-212