Bioactive Collagen Peptides

What is The History of Collagen?

The search for beauty enhancing compounds and elixirs has been occurring for millennia with collagen being one of the oldest known substances to have benefits for complexion and youth restoration.

It was two thousand years ago that Chinese Traditional Medicine first recorded the use of gelatin obtained from the hide of donkeys (Ejiao). It was used for a variety of conditions such as bleeding, dizziness, insomnia, and a dry cough but was mostly sort after for its skin hydrating and smoothing properties.

It wasn’t until the 1960’s that scientific researchers started to try to isolate the individual components of animal collagen. They identified all the individual amino acid and peptides and found they were remarkably similar in composition to human collagen.

In the 1980’s, three Polish scientists carried out pioneering experiments in the field of collagen peptide biochemistry and discovered how to effectively hydrolyse collagen to break it down into intact triple helix fibre producing peptides that were biologically active and able to synthesise collagen building blocks in the human body.

The current generation of Bioactive Collagen Peptides, consist of very specific polypeptides. They can partially survive digestion, which means they pass through the gut barrier and remain intact. Large amounts of these peptides can then get to work in the body’s target tissues that require repair and regeneration.

Recognised Targets and Mechanisms of Action

Bioactive Collagen Peptides contain high concentrations of proline and glycine, both amino acids that form strong peptide bonds making them more resistant to being broken down by our digestive enzymes. An impressive percentage of these peptides enter the bloodstream and directly stimulate connective tissue cell metabolism.

This biomaterial is composed of repetitive triplets of amino acids glycine (Gly), proline (Pro), and hydroxyproline (Hyp). Native collagen type I can be extracted from different sources, however, the main source of extraction is bovine hide because of its availability as well as its biocompatibility. Collagen extraction can be carried out from different tissues such as bones, tendons, lung tissue, or even connective tissue.

Researchers have found that collagen makes up to 35% of the whole body’s protein. Many scientists are now claiming that it could be the most important protein in the human body. This is the dry mass composition of various tissues throughout the human body:

• 75% of skin and 70% of cartilage
• 85% of tendons and 70% ligaments
• 95% of organic bone matrix (20% of total bone mass)
• 6% of the weight of muscles
• Also abundant in blood vessels, intervertebral discs, blood-brain barrier, eyes (cornea), dentin & tooth holding structures, intestine wall, fascia tissue, liver and spleen tissue.

Over 20 types of collagen have been identified, however, it is type I, II, & II collagen that make up 80-90% of the of all our body’s collagen. Collagen type I is most common in skin, bone, teeth, tendon, ligaments, vascular ligature, and organs and it gives strength to the tissue. Collagen type II is present in all joints and is the major supporting collagen of articular cartilage. Collagen type III provides flexibility to the skin, muscle, and blood vessels and is the major protein found in these tissues.

SKIN ACTIVITY

• Stimulates extracellular matrix molecules (fibrocytes) in human skin cells.
• Shows significantly higher skin elasticity after 4 to 8 weeks of treatment.
• Increases hydration of skin and lowers skin moisture evaporation.
• Improves epidermal barrier regeneration and matrix synthesis of dermal proteoglycans in aged skin.
• Improves tropo-elastin accumulation.
• Increases pro-collagen accumulation.
• Exhibits antioxidant activity by its ability to scavenge free radicals.
• Prevents oxidative damage by interrupting the radical chain reaction of lipid peroxidation.
• Produces an improvement in the structure and stratification of the epidermal layers and improves collagen fibres’ structural architecture within the dermis.
• 90 days of treatment showed that recovery from degenerative changes of the extra cellular matrix (ECM), increased stimulation for the synthesis of collagen type I, and improvements in skin firmness, texture, and hydration.
• Enhances chondrogenic gene expression. 
• Inhibits UV-B-induced pigmentation via antioxidant activity and tyrosinase inhibition.
• Decreases the expression levels of matrix metalloproteinase (MMP), which is responsible for collagen breakdown.
• Significantly increases glycosaminoglycan levels in the basal epidermis.
• Increases collagen content of the papillary dermis.
• Shows the capacity to bind Ca+ ions leading to better bioavailability, making collagen more compatible to the human body, and useful in managing mineral deficiencies.
• Collagen oligopeptides act as ligands, binding to receptors on the fibroblasts’ membrane and stimulating the production of new collagen, elastin, and hyaluronic acid. 
• Induces keratinocyte adhesion, proliferation, and differentiation and suppress wound contraction, leading to effective wound healing.
• Binds decorin protein that can indirectly block TGF-h-action within the tissue.
• Binds TGF-beta and BMP-2 action in tissue.

JOINT AND CARTILAGE ACTIVITY

• Significantly increases proteoglycan and collagen density in joints leading to improved total cartilage mass.
• Stimulates cartilage cell (chondrocytes) production.
• Shows substantial reduction in general joint pain.
• Significantly improves activity-related pain intensity.
• Improves joint mobility and range of movement.
• Counteracts the causes and symptoms of cartilage degeneration leading to improved physical performance.
• Regeneration of hyaline cartilage is observed in cultured chondrocytes.
• Shows a significantly reduction in the use of therapies like physiotherapy or ice packs after the treatment with bioactive collagen peptides (BCP).
• Induces a glycine-mediated inhibition of cytokine release.
• Increases protease activity which regulates matrix turnover by controlling catabolic pathways.

WHOLE BODY ACTIVITY

• Helps to improve memory health and improves the blood brain barrier (BBB). 
• Involved in many biological functions of the cell such as proliferation, cell survival, and differentiation.
• The synthesis of type I collagen is crucially involved in bone formation.
• Provides scaffolds as carriers of chondrocytic mesenchymal stem cells (MSCs) which bind several growth factors and cytokines. 
• Binds IGF-I and -II to the collagenous matrix of bone to reduce osteoporosis.

 

* These statements have not been evaluated by the FDA or TGA. This product is not intended to diagnose, treat, cure or prevent any disease.

Advanced Drug Delivery Reviews 55 (2003) pg1531 – 1546. Collagens—structure, function, and biosynthesis. K. Gelsea, E. Poschlb, T. Aigner. Cartilage Research, Department of Pathology, University of Erlangen-Nurnberg, Krankenhausstr. Erlangen, Germany. Department of Experimental Medicine I, University of Erlangen-Nurnberg, Erlangen, Germany

Molecules. 2019 Nov; 24(22): 4031. Published online 2019 Nov 7. doi: 10.3390/molecules24224031 Hydrolysed Collagen—Sources and Applications. Arely León-López, Alejandro Morales-Peñaloza, Víctor Manuel Martínez-Juárez, Apolonio Vargas-Torres, Dimitrios I. Zeugolis, and Gabriel Aguirre-Álvarez

Appl. Physiol. Nutr. Metab. Downloaded from cdnsciencepub.com Improvement of activity-related knee joint discomfort following supplementation of specific collagen peptides Denise Zdzieblik, Steffen Oesser, Albert Gollhofer, and Daniel König

Collagen Hydrolysates for Skin Protection: Oral Administration and Topical Formulation Antioxidants 2020, 9, 181; doi:10.3390/antiox9020181 Gabriel Aguirre-Cruz, Arely León-López , Verónica Cruz-Gómez, Rubén Jiménez-Alvarado, and Gabriel Aguirre-Álvarez

https://www.gelita.com/en/products/collagen-peptides/verisol

https://www.gelita.com/en/products/collagen-peptides/fortigel

J Nutr. 2017 Nov; 147(11): 2011–2017. Published online 2017 Oct 4. doi: 10.3945/jn.117.256404 Proline Precursors and Collagen Synthesis: Biochemical Challenges of Nutrient Supplementation and Wound Healing. Vance L Albaugh, Kaushik Mukherjee, and Adrian Barbul