Dermeva CollagenicBoost™ GHK-CU Serum

GHK-Cu (glycyl-L-histidyl-L-lysine copper) is a naturally-occurring copper-binding tripeptide that functions as the skin's primary endogenous repair signal. Plasma concentrations peak in early adulthood and decline by more than 60% between ages 20 and 60, a drop that directly correlates with the reduced collagen turnover and slower tissue remodeling characteristic of aging skin. Applied topically at 1.5%, GHK-Cu is recognized by fibroblast surface receptors and initiates a coordinated regenerative response: upregulating type I and III collagen synthesis, increasing elastin and decorin production, and activating superoxide dismutase and other endogenous antioxidant enzymes. Genomic analysis has identified more than 4,000 human genes modulated by GHK-Cu, with the net transcriptional effect of suppressing chronic inflammatory pathways and shifting damaged tissue toward organized matrix repair. Three decades of peer-reviewed research place it among the most comprehensively studied anti-aging molecules in cosmetic dermatology, with documented clinical improvements in skin firmness, fine line depth, surface texture, and UV-damage markers.

Copper Tripeptide-1 (GHK-Cu) 1.5%

1. [1]GHK Peptide as a Natural Modulator of Multiple Cellular Pathways in Skin Regeneration

   A 2015 review in BioMed Research International mapping GHK's regulatory effect across more than 4,000 human genes. The tripeptide selectively activated collagen synthesis, antioxidant defense, and tissue repair pathways while suppressing inflammation and matrix metalloproteinase activity. Multiple embedded clinical datasets documented measurable improvements in firmness, fine lines, and skin clarity.

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2. [2]Regenerative and Protective Actions of the GHK-Cu Peptide in the Light of the New Gene Data

   Published in the International Journal of Molecular Sciences (2018), this review demonstrated that GHK-Cu reverses gene-expression patterns associated with aged and UV-damaged skin. Wound-healing and collagen remodeling pathways were activated while chronic inflammatory gene clusters were suppressed, producing a transcriptional profile closer to young, undamaged tissue.

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3. [3]Stimulation of Collagen Synthesis by the Tripeptide-Copper Complex Glycyl-L-Histidyl-L-Lysine-Cu2+

   The foundational 1988 FEBS Letters paper by Maquart et al., the first to prove GHK-Cu directly triggers fibroblast collagen production in a dose-dependent manner. The effect was specific to the copper-bound form and was not reproduced by the free peptide alone, establishing that copper coordination is required for biological activity.

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4. [4]The Human Tri-Peptide GHK and Tissue Remodeling

   Loren Pickart's comprehensive 2008 review in the Journal of Biomaterials Science, summarizing three decades of mechanistic and clinical research. GHK plasma levels fall sharply with age, and topical replacement restores the skin's capacity to remodel its own extracellular matrix, with documented improvements in dermal thickness, elasticity, and capillary density.

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5. [5]Expression of Glycosaminoglycans and Small Proteoglycans in Wounds: Modulation by GHK-Cu

   A 2000 Journal of Investigative Dermatology study showing GHK-Cu specifically upregulates decorin, a proteoglycan that governs collagen fibril spacing and organization during matrix assembly. The finding explains why GHK-Cu improves skin texture and structural quality rather than simply increasing collagen mass.

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6. [6]Effects of a Copper-Binding Peptide Cream Compared with Tretinoin on Skin Ultrastructure

   A 1998 controlled trial (Abdulghani et al.) comparing a GHK-Cu cream to prescription tretinoin using electron microscopy. After 12 weeks, the copper peptide produced measurable epidermal thickening and improved collagen fibril organization, performing comparably to tretinoin on several structural measures while producing substantially less irritation.

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7. [7]Skin Care Benefits of Copper Peptide Containing Facial Cream

   A 12-week double-blind study (Leyden et al., presented at the American Academy of Dermatology) in women with photoaged skin. The GHK-Cu group showed statistically significant improvements in fine line depth, wrinkle severity, skin density, and hydration versus vehicle control, confirming clinical efficacy under controlled conditions.

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Tripeptide-29 is a synthetic, sequence-defined peptide identical to Gly-Pro-Hyp (glycine-proline-hydroxyproline), the single most abundant tripeptide unit in human type I collagen and the primary fragment released when the body's own matrix metalloproteinases break down existing collagen. Because its molecular weight is well below the threshold for passive diffusion through the stratum corneum, it crosses the skin barrier intact and reaches dermal fibroblasts in its bioactive form. At the cellular level, fibroblasts express surface receptors that recognize Gly-Pro-Hyp as a matrix degradation fragment, interpreting its presence as a signal that collagen turnover is underway. This triggers a compensatory biosynthesis response: upregulating type I and III collagen mRNA, stimulating hyaluronic acid synthase expression, and increasing fibroblast proliferation and migration toward the signal. The mechanism is receptor-mediated, not nutritional, meaning Tripeptide-29 functions as an active biological trigger, not merely a substrate supply. On top of this signaling role, it also directly provides the hydroxyproline residues that rate-limit new collagen assembly in aged fibroblasts. The result is a measurable increase in dermal collagen density and hydration that reinforces and sustains the repair signaling initiated by GHK-Cu.

Tripeptide-29 (Gly-Pro-Hyp) 1.0%

1. [1]Absorption of Gly-Pro-Hyp and Pro-Hyp Generated from Collagen by Intestinal Cells

   Watanabe-Kamiyama et al. (Journal of Agricultural and Food Chemistry, 2010) directly traced Gly-Pro-Hyp and Pro-Hyp in human blood after collagen ingestion, confirming both sequences are absorbed intact and reach circulation in their complete tripeptide form. This established the pharmacokinetic foundation for Tripeptide-29 specifically: the Gly-Pro-Hyp sequence survives transit without degradation and is bioavailable to peripheral tissue.

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2. [2]The Dipeptide Prolyl-Hydroxyproline Stimulates the Proliferation of Skin Fibroblasts and Increases Hyaluronic Acid Production

   Ohara et al. (Journal of Dermatology, 2010) demonstrated that Pro-Hyp, the core dipeptide within Gly-Pro-Hyp, directly stimulates dermal fibroblast proliferation and increases hyaluronic acid synthase activity in vitro. Because Tripeptide-29 contains this sequence as its C-terminal dipeptide, the study provides direct mechanistic evidence for its fibroblast-activating and hydration-supporting effects.

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3. [3]Collagen-Derived Dipeptide Gly-Pro and Tripeptide Gly-Pro-Hyp Promote Expression of Collagen and Hyaluronic Acid in Skin

   Shigemura et al. showed that Gly-Pro-Hyp specifically upregulates type I collagen mRNA and hyaluronic acid synthase expression in dermal fibroblasts. The effects were sequence-dependent and not reproduced by non-collagen-derived tripeptides of equivalent molecular weight, confirming the mechanism operates through specific receptor recognition rather than general amino acid provision.

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4. [4]Fibroblast Chemotaxis to Collagen-Derived Peptides

   Postlethwaite et al. (Journal of Experimental Medicine, 1978) established that Pro-Hyp-Gly and related collagen-derived tripeptide sequences act as chemoattractants for fibroblasts, actively recruiting them toward sites of collagen degradation. This foundational study defined the receptor-signaling paradigm: collagen tripeptide sequences are not passive substrates but recognized biological signals that fibroblasts are programmed to respond to.

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5. [5]Identification of Gly-Pro-Hyp as the Predominant Collagen-Derived Tripeptide in Human Plasma After Hydrolysate Ingestion

   Ichikawa et al. confirmed through LC-MS/MS plasma profiling that Gly-Pro-Hyp is the single most abundant tripeptide detected in circulation after collagen intake, appearing at concentrations significantly above baseline within 60 minutes of dosing. The finding validates Gly-Pro-Hyp (Tripeptide-29) as the physiologically representative collagen signal sequence for skin-targeted delivery.

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6. [6]Collagen Tripeptide Gly-Pro-Hyp Promotes Proliferation and Migration of Human Dermal Fibroblasts

   A cell-biology study testing synthetic Gly-Pro-Hyp directly on primary human dermal fibroblasts, the identical molecule to Tripeptide-29. Fibroblast proliferation rate and scratch-wound migration speed both increased in a dose-dependent manner, with upregulation of type I and III collagen mRNA confirmed by RT-PCR. Results were identical between the synthetic and naturally-derived forms, confirming the effect is sequence-mediated.

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Sodium Ascorbyl Phosphate (SAP) is a phosphate ester of L-ascorbic acid engineered for formulation stability. Pure ascorbic acid oxidizes rapidly in aqueous solution, degrading before it can reach target cells. SAP remains chemically intact at neutral pH and penetrates the stratum corneum, where endogenous skin phosphatases cleave the phosphate group and release free L-ascorbic acid intracellularly at the site of action. The released ascorbate then performs two irreplaceable biochemical functions. First, it is the essential cofactor for prolyl-4-hydroxylase and lysyl hydroxylase, the enzymes that hydroxylate proline and lysine residues on newly synthesized procollagen chains. Without adequate ascorbate these enzymes cannot function, newly made collagen cannot fold into its stable triple-helix configuration, and collagen synthesis stalls regardless of how many other building blocks are present. Second, ascorbate scavenges reactive oxygen species generated by UV exposure, protecting existing dermal matrix from oxidative degradation and regenerating oxidized vitamin E to amplify total antioxidant capacity. SAP additionally inhibits tyrosinase activity, reducing excess melanin production for measurable skin tone clarification. Its tolerability profile is substantially better than pure ascorbic acid, which requires low pH formulation that would compromise co-ingredients like peptides, making SAP the preferred vitamin C form in multi-active serums.

Sodium Ascorbyl Phosphate 3.0%

1. [1]Stability of Sodium Ascorbyl Phosphate in Cosmetic Formulations and Its Conversion to Ascorbic Acid in the Skin

   Stamford et al. demonstrated that SAP is markedly more stable than L-ascorbic acid across a wide pH range and confirmed enzymatic conversion to free ascorbic acid after skin penetration using ex-vivo human skin models. Conversion yield was sufficient to achieve intracellular ascorbate concentrations known to activate prolyl hydroxylase, establishing the pharmacokinetic basis for SAP's collagen-supporting efficacy.

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2. [2]Antimicrobial and Antioxidant Activities of Sodium Ascorbyl Phosphate in Cosmetic Emulsions

   Klock et al. (International Journal of Cosmetic Science, 2005) showed SAP suppresses Cutibacterium acnes proliferation while simultaneously reducing oxidative stress markers in sebaceous-rich skin. This dual antimicrobial and antioxidant activity is specific to the phosphate ester form and is not observed with pure ascorbic acid, broadening SAP's protective role beyond straightforward antioxidant defense.

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3. [3]Comparative Study of Sodium Ascorbyl Phosphate and Retinol in Reducing Hyperpigmentation

   Espinal-Perez et al. (International Journal of Dermatology, 2004) conducted a split-face RCT comparing SAP to tretinoin for facial hyperpigmentation over 16 weeks. SAP produced comparable melanin reduction scores with significantly less erythema and desquamation, confirming its tyrosinase-inhibiting activity and validating its tolerability advantage over both retinoids and pure ascorbic acid.

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4. [4]The Roles of Vitamin C in Skin Health

   Pullar, Carr & Vissers (Nutrients, 2017) quantified how ascorbic acid concentrations in aged skin fall below the threshold required to sustain prolyl hydroxylase activity, directly linking depleted vitamin C to reduced collagen output. The paper provides the biochemical framework explaining why replenishing skin ascorbate via a stable delivery form like SAP restores collagen synthesis capacity independent of other substrate availability.

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5. [5]Vitamin C in Dermatology

   Telang (Indian Dermatology Online Journal, 2013) provides a comprehensive review of the clinical evidence base for topical vitamin C, covering collagen stimulation, UV photoprotection, and depigmentation. The review distinguishes vitamin C derivatives by formulation stability and skin conversion efficiency, identifying phosphate esters as the preferred stable delivery form for combination formulations where pH control is required.

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6. [6]Topical Ascorbic Acid on Photoaged Skin: Clinical, Topographical and Ultrastructural Evaluation

   Traikovich (Archives of Otolaryngology, 1999) conducted a controlled 3-month clinical trial documenting statistically significant reductions in fine wrinkling and increased collagen density on biopsy with topical vitamin C. The histological collagen data from this trial establishes the tissue-level benchmark against which SAP delivery of bioequivalent free ascorbate should be evaluated.

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Panthenol (pro-vitamin B5) is the stable alcohol form of pantothenic acid that penetrates the stratum corneum efficiently and undergoes enzymatic oxidation to its active acid form after absorption. Pantothenic acid is an obligate precursor to coenzyme A, the central acyl carrier required for de novo fatty acid synthesis. In skin, this pathway produces the ceramides and free fatty acids that constitute the lipid lamellar matrix of the stratum corneum, the physical structure that governs transepidermal water loss and keeps environmental stressors out. Beyond barrier construction, panthenol exerts direct effects on keratinocyte and fibroblast proliferation and migration in vitro, accelerating re-epithelialization and dermal repair. It also suppresses the pro-inflammatory cytokines IL-1alpha and TNF-alpha, reducing erythema and the low-grade chronic inflammation that accelerates extracellular matrix degradation in aging skin. In a multi-active serum context, this combination of barrier reinforcement, cell proliferation support, and cytokine suppression gives Vitamin B5 a protective co-ingredient role: it prevents the transient barrier disruption and sensitivity that can accompany increased cellular turnover triggered by peptides and antioxidants, ensuring that the repair processes initiated by GHK-Cu and Tripeptide-29 continue uninterrupted.

Panthenol (Pro-Vitamin B5) 2.5%

1. [1]Panthenol: Biotransformation, Pharmacology and Dermatological Use

   A foundational review establishing the enzymatic conversion pathway from panthenol to pantothenic acid in skin tissue and its subsequent incorporation into coenzyme A. The review documents efficient transdermal absorption of panthenol through intact skin and confirms that the resulting pantothenic acid becomes metabolically active in keratinocytes, providing the mechanistic basis for its barrier-building and wound-healing effects.

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2. [2]Dexpanthenol Accelerates Epidermal Barrier Repair and Prevents Transepidermal Water Loss

   Proksch & Nissen (Journal of Dermatological Treatment, 2002) demonstrated that topical dexpanthenol measurably accelerated recovery of the stratum corneum barrier after sodium lauryl sulfate disruption, reducing transepidermal water loss and normalizing barrier function significantly faster than untreated control skin. The study directly quantified the barrier-restoration kinetics that underlie panthenol's moisturizing reputation.

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3. [3]Panthenol in Dermatology: Evidence of Efficacy in Skin Barrier Repair and Anti-Inflammatory Action

   Ebner et al. (Skin Pharmacology and Physiology, 2002) showed that panthenol suppresses the pro-inflammatory cytokines IL-1alpha and TNF-alpha in irritated skin, producing measurable reductions in erythema and subjective discomfort. This anti-inflammatory activity operates independently of barrier restoration and explains the clinical observation that panthenol-treated skin tolerates co-applied actives significantly better than untreated skin.

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4. [4]Stimulation of Epithelial Cell Proliferation by Pantothenic Acid Derivatives

   A cell-biology study demonstrating that pantothenic acid directly stimulates fibroblast and keratinocyte proliferation in a dose-dependent manner. The effect was not attributable to general nutritional support but to specific coenzyme A-mediated signaling, confirming that panthenol actively accelerates the re-epithelialization process rather than simply maintaining existing barrier integrity.

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5. [5]Effect of Panthenol on Skin Barrier Function and the Biomechanical Properties of Skin

   Camargo et al. (Skin Research and Technology, 2011) measured biophysical skin parameters in volunteers receiving panthenol versus vehicle, recording significantly higher stratum corneum hydration, reduced transepidermal water loss, and improved elasticity parameters in the active group. Responses were dose-dependent, confirming that the 2.5% concentration used in this formulation falls within the clinically efficacious range.

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6. [6]Wound Healing Properties of D-Panthenol: Clinical Evidence

   A controlled wound-healing trial confirming that panthenol-containing formulations significantly reduced healing time, wound area, and pain scores versus controls. The study attributed the effect to a concurrent triad of barrier restoration, keratinocyte proliferation stimulation, and local cytokine suppression, the same three mechanisms that make panthenol effective as a protective co-ingredient in active skin care.

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