Tripeptide-37

Tripeptide-37 (H-Arginine-Lysine-Phenylalanine-OH) is the trade and International Nomenclature of Cosmetic Ingredients (INCI) name of a simple peptide sequence used in dermatological research and the skin care industry. Though naturally synthesized in the human body, solid phase HPLC-purified isolates have been used to study their role in dermal fibroblast collagen synthesis. Recently developed suspensions of Tripeptide-37, in concert with titrations of palmitic acid and phytochemical admixtures, have also shown promise in clinical studies.
Growth modulating serum tripeptides, including Tripeptide-37, have come into prominence for their numerous biomedical applications, including anti-inflammatory and antioxidant effects, stem cell generation, wound healing, and atrophic vaginitis (decreased vaginal lubrication). These tripeptides are shown to be a key component in cell membrane signaling reactions involving TGF-β and SMAD complexes. Research also demonstrates the efficacy of palmitoyl peptides in fighting skin aging by boosting collagen and elastin production. The mechanism of Tripeptide-37 suspension therapy is two-fold: First, Tripeptide-37 mimics the natural mechanism of TGF-β to stimulate collagen synthesis; second, Tripeptide-37 suspension therapy significantly inhibits matrix metalloproteinases (MMP-9) activity.
Biochemistry of Collagen Synthesis and Matrix Metalloproteinase Deactivation
TGF-β
Members of the transforming growth factor-β (TGF-β) family are pleiotropic cytokines that have the ability to regulate numerous cell functions, including proliferation, differentiation, apoptosis, collagen synthesis, and production of extracellular matrix. TGF-β is a secreted protein that exists in at least three isoforms called TGF-β1, TGF-β2, and TGF-β3, all of which have been identified in mammals. TGF-β ligands transmit their signals to the cell’s interior via a signal transduction network involving receptor serine/threonine kinases at the cell surface and their substrates, the SMAD proteins.
SMAD Signaling
SMAD proteins are signal transducers and transcriptional modulators that mediate cellular signal pathways. The SMAD pathway is the signaling pathway that TGF-β family members signal through. In this pathway, TGF-β dimers bind to a type II receptor which recruits and phosphorylates a type I receptor. The type I receptor then recruits and phosphorylates a receptor regulated SMAD (R-SMAD). The R-SMAD then binds to the common SMAD (coSMAD) and SMAD4, forming a heterodimeric complex. The SMAD complex then moves into the nucleus where it activates or inhibits the transcription of target genes and the synthesis of, amongst other proteins, elastin, collagen I and collagen II.
Matrix Metalloproteinase: MMP Deactivation
Matrix metalloproteinases (MMP's) are enzymes that degrade extracellular matrix proteins, including collagen and elastin. MMPs also play a role in metastasis and gynecological pathology. Uterosacral ligaments disfunction and pelvic organ prolapse are two pathological processes associated with the increased expression of matrix metalloproteinases, a secondary consequence of which is atrophic vaginitis. Clinical tests using Tripeptide-37 suspension therapy has shown an ability to significantly inhibit MMP activity, which counteracts both pelvic organ prolapse and atrophic vaginitis.
Summary of Positive Clinical Research
Growth factors are well known as key regulators of the wound healing process, and their topical use has been extensively studied.
Known to play a role in collagen and elastin synthesis, recent Tripeptide-37 studies in the intimate skin care industry highlight important anti-photoaging and anti-wrinkling properties. Furthermore, increased Collagen II synthesis associated with Tripeptide-37 therapy is shown to improve vaginal lubricating properties and prevent pelvic organ prolapse by increasing smooth muscle mass and elasticity.

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