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Search Skin Biology Quick Shop  VIEW ALL PRODUCTS Shop by Skin Condition Shop by Skin Type _______________________ BEST SELLERS: • CP Serum • Super CP Serum • Super Cop Cream • Super Cop Cream 2X Strength • Super GHK-Copper • Emu Oil-S Lipid Replenisher • Two Timing Tightener • Folligen Therapy Spray • Folligen Therapy Shampoo • Folligen Nutrient Cream _______________________ • NEW! FOOT CREAM • Sebum Be Gone • Two Timing Tightener • Super GHK-Copper • LacSal Cream • LacSal Serum • Body Perfume Spray • Tin Peptide Nail Renewal TIPS ON USING SRCPS Before and After Pictures Frequently Asked Questions Order by Mail Bulk Purchases Skin Biology Policies USA Postage Rates International Postage Rates CONTACT SKIN BIOLOGY Contact Dr. Pickart Need Help Ordering Online? 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In Summary, the facts are these: 1.  The only copper peptides that have been proven - by credible skin authorities who published their results in major dermatology journals - to improve skin and hair are those invented and patented by Dr. Pickart when he was at ProCyte Corporation and the newer breakdown-resistant, long-acting copper peptides that Pickart has since developed and patented at Skin Biology. See Patents. If companies cannot send you studies on their products that were published in reputable, reviewed science journals, then do not buy the products. 2. The only copper peptides that have passed intensive and adequate safety testing are again those sold by Skin Biology, Neutrogena, and ProCyte. 3. Not all copper peptides have tissue regenerative properties. Copper peptides can be inactive or even highly toxic. Many snake venoms, bacterial toxins, insect venoms are copper peptides. 4. Some cosmetic companies use peptides produced by bacteria (such as B. Sublitis) or produced by yeast. However, such peptides can often cause allergies and respiratory problems. 5. Some companies marketing unproved copper peptides are the same companies that have been, in the past, heavily fined by the US Government for false and deceptive advertising of skin and hair products. 6. The only type of copper peptides that have tissue regenerative effects are those formed with with copper 2 ions (copper +2). Copper peptides formed with copper 1 (copper +1) have no regenerative activities on skin or hair. These are often sold as "Colorless Copper:". See copper peptide regeneration 7. Some cosmetic companies use various copper chelates such as copper EDTA, copper gluconate, or copper PCA (copper 5-oxo-L-proline, copper 2-pyrrolidine-5-carboxylic acid). Such types of complexes are usually very toxic to fibroblasts, the primary skin repair cell. 8. Many single peptides (without copper) being advertised for skin renewal appear to be similar in action to skin hardening and scar producing peptides that were extensively studied for potential uses as wound healing drugs. 9. You can buy skin and hair products based on real medical science and extensively tested for safety for the same prices as the "hype" products. There is hardly anything in the world that some man cannot make a little worse and sell a cheaper - John Ruskin >A dictionary definition of 'adulterate' (Oxford Concise Dictionary) is this: "debase by adding other or inferior substances" and Webster Unabridged adds "make impure by admixture; use cheaper, inferior, or less desirable elements in manufacture". Skin regenerating/remodeling copper peptides (SRCPs)     Skin regenerating copper peptides are the body's signal for skin regeneration and remodeling. There is no other known molecule that possesses the multiple skin repair, scar reduction, and anti-inflammatory actions of copper peptides.   Actions of SRCPs Skin Repair Increases collagen synthesis producing firmer skin Increases elastin synthesis producing more elastic skin Increases synthesis of glycosaminoglycans and proteoglycans - the skin's water holding proteins Stimulates new capillary formation for better cellular nutrition Attracts macrophages to area of application - these are the skin repair cells Removal of damaged protein and  Scar Reduction  Activates metalloproteinases that remove damaged protein Suppresses production of TGF-beta, the scar producing factor Anti-inflammatory Blocks release of oxidative iron from ferritin Blocks damaging actions of Interleukin-1 Activates inert superoxide dismutase

The peptides developed at Skin Biology were based on a fraction of soybean peptides and used to form mixtures of copper peptides that are more like the actual situation in damaged skin. This type of peptides have remarkable safety properties and are used in fluids used for intravenous feeding of hospital patients. Such peptides are also used to make synthetic milk given to newborn infants when the babies have disease conditions that make them reject their mother's milk or milk from other animals such as cows and goats.

Skin Biology Protect & Restore and BioHeal have passed numerous safety tests at the University of California at San Francisco (UCSF) and at the Shanghai Medical University. Protect & Restore has been found to be non-irritating and safe. Protect & Restore (1) was non-irritating by the human patch test (5 days of heavy covering of product on the skin), (2) was non-irritating on tape-stripped (injured) human skin, (3) passed the Ames (bacterial) test for carcinogenicity, (4) passed the guinea pig acute skin irritation test and was classified as a non-irritant, (5) passed the human induced-allergy test and classified as a non-allergen, (6) was non-comedogenic in humans and (7) was found have no evidence of oral toxicity in mice.

>Skin Damaging Copper Peptides

Many pentapeptides inhibit skin repair and hair growth

However, numerous laboratories have reported on various pentapeptides that are toxic to skin or promote tumorigenesis. This re-emphasizes why extensive safety testing and effectiveness testing is needed for any copper peptide complex that is sold for skin or hair care.

Iversen et al 1993 (Institute of Pathology, University of Oslo, Norway) reported the isolation of a pentapeptide (epidermal pentapeptide or EPP) from skin both inhibited skin repair and promoted the enhancement of skin tumorigenesis in mice. (Iversen OH, Elgjo K, Paulsen JE, Reichelt KL, Moderate enhancement of the promotion phase of skin tumorigenesis in hairless mice by topical pretreatment with a mitosis-inhibiting epidermal pentapeptide, Carcinogenesis 1993 Dec;14(12):2537-42).

Watt et al (Keratinocyte Laboratory, Imperial Cancer Research Fund, London, UK) found this pentapeptide to reduce the growth of normal skin cells but did not slow the growth of cancer cell lines such as  SV40-transformed human keratinocytes, SVK14,  squamous cell carcinoma of the oral cavity, SCC-9. (Watt FM, Reichelt KL, Elgjo K., Pentapeptide inhibitor of epidermal mitosis: production and responsiveness in cultures of normal, transformed and neoplastic human keratinocytes., Carcinogenesis 1989 Dec;10(12):2249-53)

Paus et al 1991 (Department of Dermatology, Yale University School of Medicine) found a pentapeptide from skin, pyroGlu-Glu-Asp-Ser-GlyOH, slowed the growth of mouse epidermis in vivo and of mouse keratinocytes in vitro, was isolated from mouse epidermis. It also inhibited the growth of hair follicles, using rodent in vivo and in vitro assays. (Paus R, Stenn KS, Elgjo K., The epidermal pentapeptide pyroGlu-Glu-Asp-Ser-GlyOH inhibits murine hair growth in vivo and in vitro. Dermatologica 1991;183(3):173-8

Olsen and Elgjo (Institute of Pathology, University of Oslo) reported that a single application of this pentapeptide induced a long-lasting period of reduced epidermal cell proliferation. (Olsen WM, Elgjo K., UVB-induced epidermal hyperproliferation is modified by a single, topical treatment with a mitosis inhibitory epidermal pentapeptide, J Invest Dermatol 1990 Jan;94(1):101-6)

Jensen et al (Institute of Human Genetics, University of Aarhus, Denmark) found that an number of analogs of the above pentapeptide also reduce skin repair, proliferation, and differentiation of  keratinocytes. .(Jensen PK, Elgjo K, Laerum OD, Bolund L., Synthetic epidermal pentapeptide and related growth regulatory peptides inhibit proliferation and enhance differentiation in primary and regenerating cultures of human epidermal keratinocytes.,  J Cell Sci 1990 Sep;97 ( Pt 1):51-8)

Two different types of pentapeptides, thymopentin (TP5), an active synthetic pentapeptide of thymopoietin, a naturally occurring thymic hormone and thymulin or facteur thymique serique (FTS) were found by Barbul et al (Department of Surgery, Sinai Hospital, Baltimore, MD) to inhibited wound repair (wound breaking strength and reparative collagen synthesis) in mice. (Barbul A, Shawe T, Frankel HL, Efron JE, Wasserkrug HL., Inhibition of wound repair by thymic hormones., Surgery 1989 Aug;106(2):373-6)

Strang et al (Children's Hospital, Boston, Massachusetts) wrote that a pentapeptide based on a sequence of an immune system protein (complement component C2) caused localized edema (swelling) in the skin of both guinea pigs and the humans. (Strang CJ, Cholin S, Spragg J, Davis AE 3rd, Schneeberger EE, Donaldson VH, Rosen FS., Angioedema induced by a peptide derived from complement component C2., J Exp Med 1988 Nov 1;168(5):1685-98)

Bultmann et al found that a pentapeptide from bacteria (A and B streptococci) can produce skin necrosis and immune responses in guinea pigs. Some companies use copper peptides in their cosmetics that contain peptides from other bacteria such as Bacillus Sublitis. (Bultmann B, Heymer B, Schleifer KH, Seidl HP, Haferkamp O., Migration inhibition of peritoneal macrophages by peptidoglycan.,Z Immunitatsforsch Exp Klin Immunol 1975 Jul;149(2-4):289-94)

A number of snake venoms are proteins that become toxic when combine with copper.

Huang et al (University  of Science and Technology of China, Hefei, Anhui) studied the trypsin inhibitor  E  from  black  mamba  (five-pace snake) snake venom. This peptide becomes active after complexing with copper 2. (Huang WZ; Wang C; Luo LQ; Lu ZX, Properties   of   NAD   glycohydrolase   purified  from  five-pace snake(Agkistrodon acutus) venom, Toxicon   1988,  26 (6) p535-42). Joubert and Strydom reported similar results. ( Joubert FJ; Strydom DJ, The  amino-acid  sequence  of  trypsin  inhibitor  E  of Dendroaspis polylepis polylepis (Black Mamba) venom.,Eur J Biochem   Jun 1 1978,  87 (1) p191-8)

Fini et al (Universita di Perugia, Italy) found that certain snake venoms that break DNA can be activated with zinc 2 or copper 2. (Fini C; Palmerini CA; Damiani P; Stochaj U; Mannherz HG; Floridi A, 5'-nucleotidase from bull seminal plasma, chicken gizzard and snake venom is a zinc metalloprotein., Biochim Biophys Acta   Mar 29 1990,  1038 (1) p18-22)

Peck et al that several bee venoms utilized small copper peptides such as glycylhistamine copper as part of their venom action. (Peck  ML; O'Connor R; Johnson TJ; Isbell AF; Martell AE; McLendon G; Neff RD; Wright DA, Radioprotective  potential  and  chelating properties of glycylhistamine, an analog of histamine terminal peptides found in bee venom., Toxicon   1978,  16 (6) p690-4). Ismail and Osman found scorpion venom was activated by copper 2. (Ismail M; Osman OH, Effect  of the venom from the scorpion Leiurus quinquestriatus (H & E) on histamine formation and inactivation in the rat, Toxicon   Apr 1973,  11 (3) p225-9)

Kawai et al (Tokyo   Metropolitan   Institute   for Neurosciences, Japan) reported that either zinc 2 or copper 2 enhanced the toxic activity of spider toxin on muscle nerves. (Kawai N; Miwa A; Hashimoto Y; Shudo K; Asami T; Nakajima T, Zinc  ion  enhances  the  blocking potency of synthetic analogs of spider toxin (JSTX) on the glutamate receptor., Neurosci  Res   Apr 1989,  6 (4) p358-62)

Some cosmetic companies use peptides from bacteria such as from Bacillus subtilis. Copper complexes of bacterial peptides have often been reported to
possess toxic properties.

Wright et al (National de la Sante et de la Recherche Medicale 238, Grenoble, France) reported that the deadly tetanus toxin contains copper 2 binding sites that play a role in its toxic actions. (Wright JF; Pernollet M; Reboul A; Aude C; Colomb MG, Identification   and   partial   characterization   of   a  low  affinity metal-binding site in the light chain of tetanus toxin, J Biol Chem   May 5 1992,  267 (13) p9053-8)

Bultmann et al found that a pentapeptide from bacteria (A and B streptococci) can produce skin necrosis and immune responses in guinea pigs. Some companies use copper peptides in their cosmetics that contain peptides from other bacteria such as Bacillus Sublitis. (Bultmann B, Heymer B, Schleifer KH, Seidl HP, Haferkamp O., Migration inhibition of peritoneal macrophages by peptidoglycan.,Z Immunitatsforsch Exp Klin Immunol 1975 Jul;149(2-4):289-94)

Haavik found that the antibiotic actions of metal ions, including copper 2, increased  the antimicrobial effect of bacitracin towards susceptible organisms. (Haavik HI, Possible functions of peptide antibiotics during growth of producer organisms: bacitracin and metal (II) ion transport, Acta Pathol Microbiol Scand [B] 1976 Jun;84(3):117-24)

Some bacterial peptides may cause skin reactions, allergies, and asthma. This is especially true of peptides from Bacillus subtilis that are used by some cosmetic companies.

Biagini et al (National Institute for Occupational Safety and Health, Cincinnati, OH) reported that workers who worked with B. sublitis often had 'asthma- and flu-like' symptoms, cutaneous hypersensitivity reactions, pulmonary function deficits and significantly elevated specific antibody levels.  These problems were reduced when away from work. (Biagini RE, Driscoll RJ, Bernstein DI, Wilcox TG, Henningsen GM, MacKenzie BA, Burr GA, Scinto JD, Baumgardner ES, Hypersensitivity reactions and specific antibodies in workers exposed to industrial enzymes at a biotechnology plant, J Appl Toxicol 1996 Mar-Apr;16(2):139-45)

Ciprandi et al studies 20 patients with urticaria-angioedema syndrome from food allergy. Further research indicated that this allergy was induced by proteins from Bacillus subtilis. (Ciprandi G, Scordamaglia A, Ruffoni S, Pizzorno G, Canonica GW., Effects of an adjunctive treatment with Bacillus subtilis for food allergy., Chemioterapia 1986 Dec;5(6):408-10)

Johnson et al found that six members of one family developed symptoms consistent with hypersensitivity pneumonitis after exposure to dust generated during the remodeling of their house. A detailed microbiologic investigation of the family members and the house found the family members had developed serious allergies to Bacillus subtilis. Allergies to this bacteria can produce irreversible lung damage in susceptible patients. (Johnson CL, Bernstein IL, Gallagher JS, Bonventre PF, Brooks SM, Familial hypersensitivity pneumonitis induced by Bacillus subtilis, Am Rev Respir Dis 1980 Aug;122(2):339-48)

Belin and Norman reported that commercial detergent enzymes often produced strong skin allergy weal-and-flare reactions to Bacillus subtilis. (Belin LG, Norman PS., Diagnostic tests in the skin and serum of works sensitized to Bacillus subtilis enzymes., Clin Allergy 1977 Jan;7(1):55-68) Franz et al reported similar allergies in factory workers who made commercial products based on bacteria. (Franz T, McMurrain KD, Brooks S, Bernstein IL., Clinical, immunologic, and physiologic observations in factory workers exposed to B. subtilis enzyme dust., J Allergy 1971 Mar;47(3):170-80) as did Gothe et al (Gothe, CJ, Nilzen, A, Holmgren A, Szamosi A, Werner M, Wide L, Medical problems in the detergent industry caused by proteolytic enzymes from Bacillus subtilis., Acta Allergol; 27 (1). 1972 63-86)

Some copper-peptides use yeast (yeasts are fungi) peptides and proteins. There are thousands on medical reports on allergies, atopic eczema, skin reactions, and chronic fatigue caused by yeast peptides and proteins. Below are just a few.

Orchard (Department of Dermatology, Royal Children's Hospital, Victoria, Australia) review yeast protein and peptide allergens as causative agents in pathological skin eruptions such as pityrosporum folliculitis, neonatal acne, cradle cap, eczema and food allergy. (Orchard D., Rashes in infants. Pitfalls and masquerades., Aust Fam Physician 2001 Nov;30(11):1047-51)

Brunet et al (Infectious Diseases Department-Hopital de la Croix-Rousse-69317 Lyon, France) found that yeast exposure was linked to chronic fatigue syndrome or benign myalgic encephalomyelitis. (Brunet JL, Liaudet AP, Later R, Peyramond D, Cozon GJ., Delayed-type hypersensitivity and chronic fatigue syndrome: the usefulness of assessing T-cell activation by flow cytometry--preliminary study., Allerg Immunol (Paris) 2001 Apr;33(4):166-72)

Arzumanyan et al (Mechnikov Institute of Vaccines and Sera, Russian Academy of Medical Sciences, Moscow) wrote that many patients with atopic dermatitis were allergic to a variety of fungal yeasts. (Arzumanyan VG, Magarshak OO, Semenov BF., Yeast fungi in patients with allergic diseases: species variety and sensitivity to antifungal drugs., Bull Exp Biol Med 2000 Jun;129(6):601-4)

Horner et al (Tulane University Medical Center, New Orleans, Louisiana) etimate that 6% of the population in the USA have respiratory allergies to fungi. Such allergies can produce asthma and pneumonia. (Horner WE, Helbling A, Salvaggio JE, Lehrer SB., Fungal allergens., Clin Microbiol Rev 1995 Apr;8(2):161-79)

Svejgaard et al (University Hospital of Copenhagen, Gentofte, Denmark.) reported that allergies to fungi can produce atopic dermatitis, facial erythema,  and scaling of skin. (Svejgaard E, Faergeman J, Jemec G, Kieffer M, Ottevanger V., Recent investigations on the relationship between fungal skin diseases and atopic dermatitis., Acta Derm Venereol Suppl (Stockh) 1989;144:140-2)

Small Hemolytic Copper-Amino Acid Complexes

Dimitrova et al (Institute of Physiology, Bulgarian Academy of Sciences, Sofia) wrote that amino acid - copper complexes caused hemolysis (breakdown) of both rats and human red blood cells. Such amino acids, which are the building blocks of peptides, fail to adequately bind the copper 2 and this produces red blood cell damage. This suggests that copper-peptides made from peptides that poorly bind copper could cause cellular damage. (Dimitrova D; Radonova N; Ivancheva E; Russanov E, The hemolytic effect of copper complexes with different ligands, Acta Physiol Pharmacol Bulg   1987,  13 (2) p48-53)

Copper Gluconate can be toxic

Copper gluconate is used by some companies in cosmetics and is also used as a nutrient supplement for infant foods and as an oral deodorant. Hojo et al (Department of Food Sciences and Nutritional Health, Kyoto Prefectural University, Japan) tested copper gluconate and found that serum glutamic pyruvic transaminase (SGPT) activity, an indicator of hepatotoxicity, was significantly increased compared to control in proportion to doses of CuGL. Hepatic level of glutathione measured as nonprotein sulfhydryl was not proportional to CuGL doses, but enhanced after dosing of 0.05 mmol/kg and lowered by 0.10 mmol/kg. Like SGPT activity, serum urea nitrogen (SUN) concentration, an indicator of nephrotoxicity, significantly increased in proportion to doses of CuGL. The authors suggest that copper gluconate may induce toxicity in the liver and kidney. (Hojo Y, Hashimoto I, Miyamoto Y, Kawazoe S, Mizutani T., In vivo toxicity, and glutathione, ascorbic acid and copper level changes induced in mouse liver and kidney by copper(II) gluconate, a nutrient supplement, Yakugaku Zasshi 2000 Mar;120(3):311-4)

Dangers of Copper-EDTA Complexes and Copper Sulfate

        Recently, several major cosmetic companies have been adding disodium EDTA-copper to skin creams and shampoos. These companies are apparently unaware that such complexes are toxic to skin. The National Cancer Institute, between 1960 and 1985, funded numerous research projects on the development of toxic copper complexes of the EDTA-copper type for use as anti-cancer drugs.

        This work was initiated by Prof. David Petering (at Ohio University) in the 1950's and later extended by a number of other researchers including Prof. David Petering, Jr. (the son of the first Petering) at the University of Wisconsin, the famous Linus Pauling, and even I worked on these projects.

        Complexes such as EDTA-copper are very different from tissue-regenerating peptide-copper complexes. EDTA-copper complexes are somewhat fat soluble and penetrate the cell wall, then associate with the DNA and cause DNA breakage, thus killing the cell.

        On the other hand, tissue-regenerating peptide-copper complexes carry the copper in the safe manner that the body's nutritional copper is carried through the blood to the tissues. Only peptides can do this effectively. Numerous FDA-level safety tests have established the safety of copper-peptide complexes.

        Some people have asked, "Why not just use a copper sulfate solution on the skin for renewal?" The problem here is that free copper sulfate is very irritating and once was used by physicians to remove warts from skin. Some companies have tried amino acid-copper complexes but these do not hold the copper as tightly as peptides, and skin irritation can result from the loosely bound copper. Peptides hold ionic copper approximately a million times tighter than amino acids can hold copper ion.