9064-67-9

Basic information

• Product Name: Collagen
• Synonyms: CELLAGEN(TM) BEADS;CELLAGEN(TM) SOLUTION AC-3;CELLAGEN(TM) SOLUTION AC-5;CELLAGEN(TM) SOLUTION EMEM;CELLAGEN(TM) SOLUTION PC-3;CELLAGEN(TM) SOLUTION PC-5;CELLAGEN(TM) SOLUTION T-IV;CELLAGEN(TM) SOLUTION WITH DMEM
• CAS NO: 9064-67-9
• Molecular Formula: C4H6N2O3R2.(C7H9N2O2R)n
• Molecular Weight: 0
• EINECS: 232-697-4
• Product Categories: Nutritional Supplements;API;proteins;protein
• Mol File: 9064-67-9.mol
• Article Data: 0

Chemical Properties

• Appearance: /solution
• Storage Temp.: 2-8°C
• Solubility: H2O: 5 mg/mL, hazy, colorless and viscous
• CAS DataBase Reference: Collagen(CAS DataBase Reference)
• NIST Chemistry Reference: Collagen(9064-67-9)
• EPA Substance Registry System: Collagen(9064-67-9)

Safety Data

• Hazard Codes: B
• WGK Germany: 1
• F: 10-21
• Hazardous Substances Data: 9064-67-9(Hazardous Substances Data)

Usage

Description

Collagen is an insoluble fibrous protein found extensively in the connective tissue of skin, tendons, and bones. The polypeptide chains of collagen, which predominantly contain the amino acids glycine and proline, form triple-stranded helical coils that are bound together to form fibrils, which have great strength and limited elasticity. Collagen is the foremost constituent of the extracellular matrix and is an abundant fibrous structural protein in all higher entities. It is mostly found in fibrous tissues such as skin, ligament, and tendon in the form of elongated fibrils and is also abundant in cornea, blood vessels, bone, cartilage, intervertebral disc, and the gut. Collagen is the most abundant protein in mammals, constituting over 30% of the total proteins in the animal body.

Uses

Used in Cosmetics Industry:
Collagen is used as a skin-protecting agent in skin care formulations for its strong hydration potential and its ability to bind and retain many times its weight in water. This water-binding and retention ability makes collagen effective for use in skin moisturizers. As a film former, collagen aids in reducing natural moisture loss, thereby helping hydrate the skin. In skin care preparations, it enhances the humectancy of a topical product, contributes sheen, builds viscosity, and leaves the skin smooth and soft.
Used in Detergent Industry:
Collagen is used in detergents to significantly reduce the amount of amino acids extracted from the skin when washing with the detergents and water.
Used in Food Industry:
Collagen is used as a supplement in food products to enhance their nutritive and functional properties, resulting in improved health benefits. Collagen supplements help fulfill the collagen requirement of the body. In the food industry, collagen is extensively used as foaming agents, emulsifiers, stabilizers, microencapsulating agents, and biodegradable film-forming materials.
Used in Pharmaceutical and Medical Applications:
Collagen is considered an excellent biomaterial for the development of wound dressing systems and tissue engineering constructs due to its exceptional biocompatibility, low antigenic, and high direct cell adhesion ability. For medical applications, collagens are processed into various forms such as sheets, scaffolds, tubes, films, sponges, membranes, composites, fleeces, injectable solutions, and dispersions. Collagen has been applied for drug delivery in numerous applications such as ophthalmology, wound and burn dressing, tumor treatment, and tissue engineering.
Used in Agricultural Applications:
Collagen is used in agricultural applications due to its insoluble fibrous protein nature found extensively in the connective tissue of skin, tendons, and bones. The polypeptide chains of collagen predominantly contain glycine and proline, which form triple-stranded, helical coils to form fibrils with strength and elasticity.

Properties

Collagen fibers are commonly white, opaque, and readily recognized in tissues. It is considered as a viscoelastic material that possesses high tensile strength and low extensibility. Its isoelectric point is around pH 5.816; and in terms of temperature, the shrinkage temperature[Ts] of most mammalian fibrils is between 62°C and 65°C, whereas fish fibrils Ts ranges from 38°C to 54°C. On the other hand, the denaturation temperature Tm is less by 25°C 30°C than Ts[5]. It is known that collagen is a molecule with low immunogenicity, diminishing the possibilities of not being accepted when ingested or injected to a foreign body. The only fractions capable of occasioning immune response are located in the helical region of the chains and in the telo-peptide region[6]. Even though this molecule has low antigenicity, it can be modified to eliminate any immune response. An alternative can be carried out by the elimination of banded structure through heat or chemical treatment degradation of non-helical section by proteinases or cross-linking[7, 8].

Structure

Three identical or non-identical polypeptide chains form the distinct structure of collagen. Each chain is composed of around 1000 amino acids or more in length in some collagen types[9]. Super coiling of three polypeptide chains in a left handed manner around a common axis, with staggering of one residue between the adjacent chains leads to a single extended right-handed triple helical conformation. Glycine is the only amino acid that can be accommodated in the interior part of the triple helix without chain distortion. The close packing of three chains around a common axis leads to a steric constraint on every third residue. N, C-telopeptides are the non-helical terminals of triple helix that perform a significant role in the formation of micro-fibril and fibril. The arrangement of amino acids in a unique fashion leads to formation of triple-helical structure of collagen. Glycine is having the smallest side group and is repeated at every third location in the order; it permits close packaging of the chains into a helix and leaves very minute space for residues in the core. In the repeating unit of Gly-X-Y, around 35% of the non-glycine positions are engaged by proline which is almost exclusively found in the X-position while Y-positions are predominantly occupied by 4-hydroxyproline. Prolyl hydroxylase converts proline of into hydroxyproline by post-translational hydroxylation[10]. Hydroxyproline comprises around 10% of the amino acid composition of collagen that can be readily used for the quantification of collagen or its degraded products in the presence of other proteins[11]. Along with hydroxyproline collagen also have the presence of unusual amino acid hydroxylysine. Hydroxylysine is formed from lysine by enzymatic hydroxylation through lysyl-hydroxylase; which is exactly similar to the conversion of proline to hydroxyproline. Hydroxylysyl residues provide the attachment of sugar components that is very vital for the formation of triple-helical structure of the collagen molecule[12].

Resources

Collagen and gelatin are different forms of the same macromolecule. Gelatin is a soluble protein obtained by partial hydrolysis of collagen. In recent times applications of collagen and gelatin in the field of food, cosmetic, photographic, medicine and cell cultures have increased. Most of the times the collagen and gelatin used in the industrial products are obtained from mammalian sources[bovine and porcine] whereas; production of collagen and gelatin from the fish waste has received considerable attention in recent years[13]. Nature sources Collagen sources can be obtained from animal and vegetable sources. From animal sources, the most common are bovine, porcine, human collagen, and marine organism such as scale fish and fish skin[4, 14-16]. Among these animal sources, bovine collagen is commonly used as a temporary cover for extra-oral wounds[17] and also for the burns on the body. It has large applications because of its helpfulness and biocompatibility[18]. Porcine collagen matrices, on the contrary, have the potential to be useful for grafting of soft tissues[19]. It provides a biocompatible surgical material as an alternative to an autogenous transplant[20]. Animal terrestrial sources comprise from chicken, kangaroo tail, rat tail tendons, duck feet, equine tendon, alligators bon/skin, bird’s feet, sheepskin, and frog skin. Types I and II come from equine skin, cartilage, and flexor. Types I, II, III, and V come from chicken neck. Type IX is found in chicken embryo sternal cartilage, I and III from skin, and IV from muscular tissue[21]. Synthetic sources Collagen is widely used to help blood clotting, healing, and tissue remodeling. Animal-derived[natural] collagen is used in many clinical applications, but there are some concerns with respect to its role in inflammation, batch-to-batch variability, and possible disease transfection[6]. To avoid immune problems, some synthetic sources have been found, for example, the material commercially named KOD. This is a synthetic protein made of 36 amino acids that self-assemble into triple-helix nanofibers and hydrogels; it mimics natural collagen and it could improve upon commercial sponges or therapies based on naturally derived collagen. The sequence of the peptide is[Pro-Lys-Gly][Pro-Hyp-Gly][Asp-HypGly], and in single-letter amino acid, abbreviation is[P-K-G][P-OG][D-O-G], giving it the name KOD[6]. This material presents theoretical analogues to native collagen in protein structure and folding, as well as pro-coagulatory fractions that could promote platelet activation and adhesion[6]. It can be used as a hemostat or a clotting agent thanks to its capacity to trap red blood cells to stop bleeding. It also binds and activates platelets to form clots and promote healing without promoting inflammation[22]. Another synthetic source for collagen has been developed using recombinant technology to produce high quality and animal-derived contaminant-free collagens. These recombinant collagens have been produced in mammalian cells, insect cell cultures, yeast, and mostly in plant cell culture. The production of plant-derived recombinant collagen has been reported using tobacco, transgenic maize seed, and barley[23].

References

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Biochem/physiol Actions

Collagen provides extracellular support for multicellular animals. Collagen type I offers mechanical stability, strength and toughness to a range of tissues from tendons and ligaments, to skin, cornea, bone and dentin.