Dipeptide-6 is a dipeptide formed through a peptide bond linking proline (Pro) E hydroxyproline (Hyp). Considered one of the primary characteristic peptide fragments produced during the digestion and subsequent breakdown of collagen within the human body, it serves as a near-constant biomarker of collagen metabolism. Hydroxyproline itself is an amino acid unique to collagen; the stability and various forms of biological activity associated with this dipeptide depend heavily on its presence – maintaining at least partial structural integrity of the skin being one such outcome.
Sequenza
H-Pro-Hyp-OH
Numero CAS
18684-24-7
Formula molecolare
C₁₀H₁₆N₂O₄
Peso Molecolare
228.25 g/mol
Research Of Dipeptide-6
Collagen is the primary structural protein found in most connective tissues (skin, bones, cartilage being prime examples). Characteristic repeating sequences (Gly-X-Y, X/Y again typically Pro or Hyp) give these tissues their desired elasticity and all round mechanical strength. Hydroxyproline as mentioned is that defining amino acid, its content a near real time reflection of the body’s current metabolic state regarding collagen.
Hydroxyproline containing peptide segments are the key bioactive parts of any collagen derived peptide – Pro-Hyp and related forms being well documented. Oral administration allows for some level of absorption, entering the bloodstream to at least partially regulate skin fibroblast function.
Dipeptide-6 is a naturally occurring peptide, derived from said collagen. Animal sourced collagen (fish skin, bovine etc.) undergoes both human and industrial digestion/hydrolysis; long chains break down into small peptides, H-Pro-Hyp-OH being one of the more easily detected bioactive end products.
Research into its mechanism is currently pointing towards the anti-aging effects of dipeptide-6 as being directly related to the stimulation of fibroblast proliferation and activity.
Promoting Fibroblast Proliferation and Collagen Synthesis: Fibroblasts are the primary ‘factories’ responsible for synthesizing the skin scaffolding and hydrating components; collagen, elastin, and hyaluronic acid being the most well-documented examples. Their active function significantly declines with age.
Multiple in vitro studies consistently show that Dipeptide-6 effectively activates fibroblast proliferation and subsequent migration. Research specifically points to Dipeptide-6 stimulating this proliferation and growth – mouse and human skin fibroblasts both responding to it.
A chemotactic aspect is also observed, fibroblasts being attracted to move towards certain areas; repair of skin damage and various forms of tissue remodeling depend on this process.
Dipeptide-6 has been shown to significantly enhance hyaluronic acid synthase activity within fibroblasts. Directly related to the above, improved skin hydration (a plumper, near-dewy appearance) results from increased production.
A randomized, in doppio cieco, placebo controlled clinical trial using a high concentration collagen peptide formulation containing Pro-Hyp demonstrated improvements in facial skin hydration, elasticity, wrinkles and roughness metrics over 8 settimane.
Promoting ECM Regeneration and Remodeling: Activating fibroblasts as mentioned above, indirect ECM regeneration is a key outcome. Upregulation of specific ECM proteins (type I collagen being the prime example, along with elastin and fibronectin) at the genetic level has been reported.
Inhibition of Matrix Metalloproteinase-1 (MMP-1) Expression: Oral supplementation of collagen peptides leads to increased plasma levels of Gly-Pro and all related dipeptides; reducing UVB induced MMP-1 is one of the more measurable end points of this pathway.
Dipeptide-6, in all its forms, is a true multi-faceted regulator of skin physiology. Facial aging is only one of many potential benefits of Pro-Hyp or similar dipeptides.
COA
HPLC
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