Collagen

Collagen (/ˈkɒlədʒən/) is the main structural protein in the extracellular matrix of a body's various connective tissues. As the main component of connective tissue, it is the most abundant protein in mammals.^[1] 25% to 35% of a mammalian body's protein content is collagen. Amino acids are bound together to form a triple helix of elongated fibril^[2] known as a collagen helix. The collagen helix is mostly found in connective tissue such as cartilage, bones, tendons, ligaments, and skin. Vitamin C is vital for collagen synthesis, while Vitamin E improves its production.

Depending upon the degree of mineralization, collagen tissues may be rigid (bone) or compliant (tendon) or have a gradient from rigid to compliant (cartilage). Collagen is also abundant in corneas, blood vessels, the gut, intervertebral discs, and the dentin in teeth.^[3] In muscle tissue, it serves as a major component of the endomysium. Collagen constitutes 1% to 2% of muscle tissue and accounts for 6% of the weight to skeletal muscle.^[4] The fibroblast is the most common cell creating collagen in a body. Gelatin, which is used in food and industry, is collagen that was irreversibly hydrolyzed using heat, basic solutions, or weak acids.^[5]

^ Di Lullo GA, Sweeney SM, Korkko J, Ala-Kokko L, San Antonio JD (February 2002). "Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen". The Journal of Biological Chemistry. 277 (6): 4223–4231. doi:10.1074/jbc.M110709200. PMID 11704682.
^ "Leather grown using biotechnology is about to hit the catwalk". The Economist. 26 August 2017. Archived from the original on 1 September 2017. Retrieved 2 September 2017.
^ Britannica Concise Encyclopedia 2007
^ Sikorski ZE (2001). Chemical and Functional Properties of Food Proteins. Boca Raton, Florida: CRC Press. p. 242. ISBN 978-1-56676-960-0.
^ Bogue RH (1923). "Conditions Affecting the Hydrolysis of Collagen to Gelatin". Industrial and Engineering Chemistry. 15 (11): 1154–59. doi:10.1021/ie50167a018.

[1] Di Lullo GA, Sweeney SM, Korkko J, Ala-Kokko L, San Antonio JD (February 2002). "Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen". The Journal of Biological Chemistry. 277 (6): 4223–4231. doi:10.1074/jbc.M110709200. PMID 11704682.

[2] "Leather grown using biotechnology is about to hit the catwalk". The Economist. 26 August 2017. Archived from the original on 1 September 2017. Retrieved 2 September 2017.

[3] Britannica Concise Encyclopedia 2007

[4] Sikorski ZE (2001). Chemical and Functional Properties of Food Proteins. Boca Raton, Florida: CRC Press. p. 242. ISBN 978-1-56676-960-0.

[5] Bogue RH (1923). "Conditions Affecting the Hydrolysis of Collagen to Gelatin". Industrial and Engineering Chemistry. 15 (11): 1154–59. doi:10.1021/ie50167a018.

[1]

[2]

[3]

[4]

[5]