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Collagen is the foremost constituent of the extracellular matrix that is 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. These are the most abundant protein in mammals constituting over 30% of the total proteins in animal body. All proteins that have a structure based on three helix polypeptide chains belonging to the collagen family, being identified 26 types until now. The unique structure of collagen is responsible for its fibrous nature that is very hard to degrade. Until now, the molecule has been classified in 26 different types that are grouped into eight families depending on its structure, chain bonding, and position in the human body. Among the classifications, it can be found the fibril-forming, basement membrane, microfibrillar, anchoring fibrils, hexagonal network-forming, fibril-associated collagens with interrupted triple helix [FACIT], transmembrane, and multiplexins

Collagen is the main structural protein of the various connective tissues in animals.(The name collagen comes from the Greek kolla meaning glue and suffix -gendenoting producing.) As the main component of connective tissue, it is the most abundant protein in mammals, making up from 25% to 35% of the whole-body protein content. Collagen, in the form of elongated fibrils, is mostly found in fibrous tissues such as tendons, ligaments and skin, and is also abundant in corneas, cartilage, bones, blood vessels, the gut, and intervertebral discs. The fibroblast is the most common cell that creates collagen. In muscle tissue, it serves as a major component of the endomysium. Collagen constitutes one to two percent of muscle tissue, and accounts for 6% of the weight of strong, tendinous muscles. Gelatin, which is used in food and industry, is collagen that has been irreversibly hydrolyzed.