WHAT IS COLLAGEN?
Collagen is a fundamental structural material in vertebrates and one of the most abundant proteins in the human body. It is commonly found in tissues with mechanical functions, providing durability by forming supportive networks within cellular structures. Collagen can be sourced from bovine, porcine, marine sponges, jellyfish, fish skin, and human collagen.
Collagen has a molecular weight of approximately 300 kDa, a diameter of 14-15 Å, and a length of 2800 Å. It is structured as a triple-helix conformation composed of three polypeptide chains known as α-chains.
Collagen is a multifunctional protein, playing a vital role in medical devices, pharmaceuticals, biomedical applications, cosmetics, and the food industry. Its unique properties include high water absorption capacity, superior biocompatibility, low immunogenicity, biodegradability, high porosity, easy processability, lipid-free surface penetration, and natural compatibility with synthetic polymers.
APPLICATIONS OF COLLAGEN
Biomedical Engineering:
Collagen is used in medical devices, implant materials, periodontal treatments, and in the production of artificial tissues and organs (e.g., artificial vessels, bone grafts).
Pharmaceutical Products:
Collagen is included in formulations such as supplements supporting skin and joint health, available in capsule or tablet form.
Dermal Fillers:
As a protein that enhances skin elasticity, collagen is used as a dermal filler to smooth wrinkles for younger-looking skin.
Cell Carrier and Support Material:
Due to its biocompatibility, collagen is employed in cartilage and bone cell cultures, promoting cell growth and proliferation.
Artificial Bone and Cartilage Production:
Collagen is utilized in tissue engineering to regenerate bone and cartilage. It provides a matrix for cells to organize and form new tissues.
Use in Implants and Grafts:
Collagen matrices repair cartilage damage and recover bone tissue loss, often found in surgical materials, artificial bone grafts, and implants.
Wound Healing and Regeneration:
Collagen assists in repairing and regenerating injured tissues. Its 3D structure is particularly effective in healing bone fractures, torn cartilage, and burn wounds.
Joint Health and Treatments:
Collagen supports joint health and is widely used as a supplement or in intra-articular injection therapies for joint disorders like osteoarthritis.
Cosmetic Industry:
Collagen enhances skin elasticity and hydration, reducing wrinkles and promoting a healthy, youthful appearance, making it a key ingredient in many cosmetic products.
Dietary Supplements:
As a naturally occurring protein in the body, collagen is included in supplements to support joint health, strengthen bones, and improve hair, skin, and nail health.
TYPES OF COLLAGEN
Telocollagen:
Telocollagen retains the telopeptide regions (N-terminal and C-terminal) through acidic extraction, resulting in more stable collagen fibers with superior mechanical properties for tissue durability.
Atelocollagen:
Atelocollagen is produced by removing the telopeptide regions, reducing immunogenicity and making it less likely to provoke an immune response. It is commonly used in medical devices, tissue engineering, and cosmetics.
Undenatured Collagen:
Also known as "UC" or "native collagen," it is extracted at low temperatures to preserve its natural structure and functionality. It is commonly used in dietary supplements for joint health due to its high efficacy.
Hydrolyzed Collagen:
This refers to peptides obtained through enzymatic processes or strong acids/alkalines, breaking collagen into smaller, easily digestible parts. It is used in medical devices and dietary supplements for joint health and in cosmetics to enhance skin elasticity and reduce aging signs.
Gelatin:
Formed by the thermal denaturation of collagen, gelatin is a single polypeptide with a random coil structure. It is commonly used in the food industry for jelly production, confectionery, and other applications.
DIFFERENCES BETWEEN TELOCOLLAGEN, ATELOCOLLAGEN, UNDENATURED COLLAGEN, AND HYDROLYZED COLLAGEN
Collagen molecules contain a triple-helix region and non-helical telopeptide regions at the N-terminal and C-terminal. These telopeptide regions, consisting of two α1 chains and one α2 chain, are conserved across species and exhibit low immunogenicity. Removing the telopeptide regions with protease enzymes results in atelocollagen, retaining the properties of collagen with reduced immunogenicity.
Heat denaturation of collagen or atelocollagen's triple-helix structure produces gelatin. Hydrolyzed collagen is obtained by breaking down collagen using strong acids, strong alkalines, or enzymatic methods, creating peptides widely used in dietary and cosmetic applications.
| BUGA-CoL Atelocollagen | More Information | |
| Undenatured Collagen | More Information | |
| Hydrolyzed Collagen | More Information | |
| Fibrillar Collagen | More Information | |
| Marıne Collagen | More Information | |
| Sponge Collagen | More Information | |
| Telocollagen | More Information |
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