Matrikine Peptides
Overview
Matrikine peptides are bioactive fragments released from extracellular matrix proteins during tissue remodeling or injury. These sequences, derived from collagen, elastin, fibronectin, and laminin, regulate cellular processes including migration, proliferation, and differentiation by binding to cell surface receptors. Matrikines serve as endogenous signals coordinating wound healing and tissue homeostasis.
Key Research Findings
Preclinical research has identified multiple matrikine sequences with distinct activities, such as the elastin-derived VGVAPG hexapeptide promoting chemotaxis and the collagen-derived DGEA sequence supporting cell adhesion. In vitro and animal models have demonstrated roles in angiogenesis, inflammation resolution, and matrix synthesis. Clinical translation has been limited to topical cosmetic applications, with no approved pharmaceutical indications.
Topical, Subcutaneous injection
Research Phase
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Find a Matrikine Peptides ProviderRelated Peptides
BPC-157
Research PhaseA synthetic gastric pentadecapeptide derived from a protein found in human gastric juice. BPC-157 promotes angiogenesis and the expression of growth factors including VEGF, EGF, and NO-mediated pathways. It has demonstrated cytoprotective and wound-healing properties across multiple tissue types in preclinical models, including tendon, muscle, ligament, and gastrointestinal mucosa.
TB-500 (Thymosin Beta-4)
In Clinical TrialsThymosin Beta-4 is a 43-amino acid actin-sequestering protein involved in cell migration, differentiation, and tissue repair. It promotes wound healing by upregulating cell-building proteins such as actin and laminin, facilitating cell migration to sites of injury. TB-500 also has anti-inflammatory properties mediated through NF-kB pathway modulation.
GHK-Cu
Research PhaseA naturally occurring copper-binding tripeptide (glycyl-L-histidyl-L-lysine) found in human plasma, saliva, and urine. GHK-Cu activates tissue remodeling by stimulating collagen synthesis, glycosaminoglycan production, and angiogenesis while suppressing fibrinogen synthesis. It modulates the activity of matrix metalloproteinases and influences over 4,000 genes related to tissue repair.
DSIP (Delta Sleep-Inducing Peptide)
Research PhaseA naturally occurring nonapeptide (Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu) originally isolated from cerebral venous blood of rabbits during induced sleep. DSIP modulates sleep architecture by promoting delta wave (slow-wave) sleep through interactions with the GABAergic system and hypothalamic sleep centers. It also exhibits stress-protective, analgesic, and neuromodulatory properties.