Biotinoyl Tripeptide is a synthetic compound formed by linking biotin (vitamin H) with the tripeptide Gly His Lys (GHK) through an amide bond. The structural advantage of this substance enables biotin to enhance cellular function at the metabolic support level, while GHK activates repair programs at the signaling regulation level, forming a three-dimensional network of "nutrient supply+gene regulation". As a lipophilic group, biotin can enhance the ability of peptides to penetrate the stratum corneum, and achieve precise enrichment of drugs in hair follicles, sebaceous glands, and other appendages through the biotin avidin system. Chemical modification reduces the enzymatic hydrolysis rate of GHK in vivo and prolongs its half-life. This substance promotes the deposition of basement membrane collagen IV by activating the expression of COL4A1 gene in fibroblasts. Collagen IV is the main component of the basement membrane, and its increase can enhance the strength of the epidermal dermal junction and reduce wrinkle formation.
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Biotinoyl Tripeptide-1 COA
Synergistic induction of type IV collagen and laminin 5
In the biological research of skin and hair follicles, the dynamic balance of extracellular matrix (ECM) is the core of maintaining tissue structural stability and functional integrity. Type IV collagen and laminin 5, as key components of the basement membrane, anchor the epidermis and dermis through the formation of a three-dimensional network structure, and regulate cell proliferation, migration, and differentiation. Biotinoyl Tripeptide (BTP-1), as a synthetic bioactive peptide, significantly enhances the hair follicle dermal junction strength by specifically stimulating the synthesis of type IV collagen and laminin 5, making it a hot molecule in the fields of hair loss prevention, hair growth promotion, and skin repair.
Molecular characteristics and biological functions
Biotinoyl Tripeptide-1(BTP-1)
BTP-1 is a synthetic compound formed by covalent bonding of biotin (vitamin H) and tripeptide Gly His Lys (GHK) through amide bonds. Its molecular formula is C24H38N8O6S and its molecular weight is 566.67 Da. Its structure consists of three functional domains:
Biotin part: As a water-soluble vitamin, it participates in fat and protein metabolism, and acts as a carboxylase coenzyme to promote collagen synthesis;
GHK tripeptide: belongs to the Matrikine series (hydrolyzed products of skin matrix after injury), which can activate the expression of cell repair genes and regulate connective tissue reconstruction;
Amide bonding: enhances molecular stability and ensures synergistic effects between biotin and GHK.
Promote ECM synthesis: By upregulating the gene expression of type IV collagen and laminin 5, enhance the strength of hair follicle dermal junction;
Antioxidant protection: Clearing reactive oxygen species (ROS) from hair follicles and reducing hair follicle atrophy induced by oxidative stress;
Nutrient delivery: As a carrier, it precisely transports nutrients such as biotin to hair follicle cells, promoting keratin synthesis;
Cellular signal regulation: binds to surface receptors of hair follicle cells, activates pathways such as PI3K/AKT and Wnt/β - catenin, and promotes proliferation of hair follicle cells.
Type IV collagen
Type IV collagen is the main component of the dense layer of the basement membrane, accounting for over 50% of the total basement membrane protein. Its molecule is composed of three alpha chains (α 1- α 6) forming a triple helix structure, which is cross-linked between molecules to form a continuous three-dimensional mesh. It has the following characteristics:
Non fibrous structure: Unlike the fibrous structure of type I and III collagen, type IV collagen is spherical or rod-shaped, which is more suitable for the mesh structure of the basement membrane;
Non collagenous domain (NC1): located at the molecular end, involved in cell adhesion, signal transduction, and intermolecular cross-linking;
Dynamic regulation: During pathological processes such as liver fibrosis and skin aging, the expression level of type IV collagen changes significantly, reflecting the degree of tissue damage.
Structural support: forms a composite grid with laminin 5, nestin, etc. to maintain the stability of the basement membrane;
Cell anchoring: Connecting with epidermal keratinocytes through integrin receptors to fix the epidermis to the dermis;
Signal center: stores and releases growth factors (such as TGF - β, EGF) to regulate cell proliferation and differentiation.
laminin 5
Laminin-5 is the core glycoprotein of the transparent layer of the basement membrane, composed of three peptide chains - α 3, β 3, and γ 2- forming a cross shaped trimer with a molecular weight of approximately 460 kDa. Its structure includes multiple functional domains:
G-domain: located at the end of the α 3 chain, mediating cell adhesion and migration;
EGF like repetitive sequence: involved in extracellular matrix cross-linking;
Short arm structure: It combines with type VII collagen to form anchoring filaments, which penetrate the basement membrane and connect to the dermal papilla layer.
Epidermal dermal anchoring: fixing the epidermis to the dermis through the interaction of anchor wires with type VII collagen and nestin;
Collaborative mechanism
BTP-1 regulates the synthesis of type IV collagen and laminin 5
Biotinoyl Tripeptide synergistically induces the synthesis of type IV collagen and laminin 5 through the following pathways:
The role of GHK tripeptide: As a Matrikine, GHK can bind to the surface receptors of hair follicle cells, activate the MAPK/ERK pathway, and promote the transcription of COL4A1 (type IV collagen alpha 1 chain) and LAMA3 (laminin 5 alpha 3 chain) genes;
Synergistic effect of biotin: As a carboxylase coenzyme, biotin enhances the activity of collagen synthase, further amplifying the induction effect of GHK.
Experimental evidence:
In an in vitro hair follicle organ culture model, after 48 hours of treatment with 100 ppm BTP-1, the mRNA expression levels of type IV collagen and laminin 5 increased by 2.3 times and 1.8 times, respectively;
In clinical studies, after 12 weeks of use of shampoo containing 0.05% BTP-1, the deposition of type IV collagen on the scalp of subjects increased by 35%, and the expression of laminin 5 increased by 28%.
Enhanced protein synthesis and secretion
MTOR pathway activation: BTP-1 promotes protein synthesis in hair follicle cells through the PI3K/AKT/mTOR pathway, increasing the secretion of type IV collagen and laminin 5;
Endoplasmic reticulum stress relief: Biotin partially maintains endoplasmic reticulum calcium homeostasis, reduces protein folding errors, and improves ECM protein secretion efficiency.
Animal experiments:
In the C57BL/6 mouse hair loss model, after 8 weeks of local application of BTP-1 (500 ppm), the immunofluorescence intensity of type IV collagen and laminin 5 around the hair follicles increased by 42% and 37%, respectively, and the hair growth density increased by 55%.
The interaction between type IV collagen and laminin 5
Type IV collagen and laminin 5 form a stable basement membrane structure through the following mechanisms:
NC1 domain binds to G domain: The NC1 domain of type IV collagen interacts with the G domain of laminin 5 through non covalent bonds, forming a "collagen laminin" complex;
Nestin bridging: Nestin-1/2 simultaneously binds to type IV collagen and laminin 5 through its globular domain, forming a three-dimensional mesh scaffold.
Structural biology evidence:
Cryo electron microscopy analysis shows that the triple helix of type IV collagen binds to the short arm of laminin 5 in a ratio of 1:2, forming a mesh structure with a diameter of approximately 15 nm;
X-ray diffraction analysis confirmed the existence of specific binding sites between the EGF like repeat sequence of Nestin and the NC1 domain of type IV collagen.
Signal Transmission Coordination
Integrin receptor activation: Type IV collagen and laminin 5 jointly activate the FAK/Src pathway through the α 6 β 4 integrin receptor, promoting hair follicle stem cell proliferation;
Growth factor release: Type IV collagen grid stores TGF - β 1, and laminin 5 binds to EGF through the G domain, synergistically regulating hair follicle differentiation.
Functional experiment:
In the three-dimensional skin equivalent model, when both type IV collagen and laminin 5 are added simultaneously, the hair follicle induction efficiency is increased by 2.1 times compared to adding either component alone;
After blocking the α 6 β 4 integrin, the BTP-1-induced hair follicle growth effect disappeared, confirming the synergistic effect of type IV collagen and laminin 5 signaling.
The antioxidant and nutrient transport effects of BTP-1
ROS clearance: The biotin portion in BTP-1 reduces ROS levels in hair follicles by regenerating glutathione (GSH), thereby reducing oxidative damage to type IV collagen and laminin 5;
MMPs inhibition: GHK tripeptide can downregulate the expression of matrix metalloproteinases (MMP-2/9), preventing ECM degradation.
Clinical data:
In androgenic alopecia patients, after 16 weeks of using BTP-1 containing essence solution, the scalp MDA (malondialdehyde, a marker of oxidative stress) level decreased by 41%, and the degradation products of type IV collagen and laminin 5 decreased by 33%.
Precise delivery of nutrients
Biotin carrier effect: BTP-1 is internalized through the biotin receptor (SMVT) on the surface of hair follicle cells, while carrying trace elements such as zinc and copper into the cells, promoting keratin synthesis;
Blood supply improvement: BTP-1 can induce the expression of vascular endothelial growth factor (VEGF), increase the density of capillaries around hair follicles, and improve nutrient supply efficiency.
Animal model:
In the nude mouse skin transplantation model, the microvascular density around hair follicles in the Biotinoyl Tripeptide treatment group was 2.8 times higher than that in the control group, and the survival rate of transplanted hair follicles increased by 60%.
Frequently Asked Questions
What is biotinoyl tripeptide?
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A tripeptide complex with biotin - vitamin H, designed to prevent hair loss, stimulates the metabolism of hair follicle cells, promotes hair and eyelash growth. Works to activate tissue repair gene expression.
Is biotinoyl tripeptide-1 the same as biotin?
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Biotinoyl tripeptide-1 is a peptide-enhanced form of biotin that penetrates hair follicles deeply and boosts keratin production. It has been clinically proven to increase hair density and strength.
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