Collagen is a complex molecule with a triple helix structure, made up of three polypeptide chains coiled together. There are at least 28 different types of collagen, but 90% of the collagen in the human body is of Type I.

Main Types. Beyond Type I, Types II and III are the most prevalent. Type II collagen is primarily found in cartilage, whereas Type III mostly supports muscle structures, organs, and arteries.

Synthesis. Collagen is synthesized in cells called fibroblasts. This process starts with producing collagen precursors called procollagens.

Degradation and Renewal. As one ages, collagen structures break down, and the body's ability to produce new collagen diminishes. Factors like sun exposure, smoking, and a poor diet can accelerate this degradation.

Applications in Medicine. Due to its unique properties, collagen is utilized in various medical treatments, including plastic surgery, burn treatment, and arthritis.

Dietary Supplementation. Many products, like bone broths and supplements, are marketed for their richness in collagen, promising benefits like younger-looking skin and stronger joints.

Collagen and gelatin have been widely used in the food, pharmaceutical, and cosmetic industries due to their excellent biocompatibility, easy biodegradability, and weak antigenicity.

Collagen studies

Collagen is a fibrillar protein that conforms the conjunctive and connective tissues in the human body, essentially skin, joints, and bones. This molecule is one of the most abundant in many of the living organisms due to its connective role in biological structures. Due to its abundance, strength and its directly proportional relation with skin aging, collagen has gained great interest in the cosmetic industry (1).

Collagen and gelatin have been widely used in the food, pharmaceutical, and cosmetic industries due to their excellent biocompatibility, easy biodegradability, and weak antigenicity. Fish collagen and gelatin are of renewed interest, owing to the safety and religious concerns of their mammalian counterparts. The structure of collagen has been studied using various modern technologies, and interpretation of the raw data should be done with caution. The structure of collagen may vary with sources and seasons, which may affect its applications and optimal extraction conditions. Numerous studies have investigated the bioactivities and biological effects of collagen, gelatin, and their hydrolysis peptides, using both in vitro and in vivo assay models. In addition to their established nutritional value as a protein source, collagen and collagen-derived products may exert various potential biological activities on cells in the extracellular matrix through the corresponding food-derived peptides after ingestion, and this might justify their applications in dietary supplements and pharmaceutical preparations. Moreover, an increasing number of novel applications have been found for collagen and gelatin (2).

References______________________________________________________________________

(1) Avila Rodríguez MI, Rodríguez Barroso LG, Sánchez ML. Collagen: A review on its sources and potential cosmetic applications. J Cosmet Dermatol. 2017 Nov 16. doi: 10.1111/jocd.12450.

(2) Liu D, Nikoo M, Boran G, Zhou P, Regenstein JM. Collagen and gelatin  Annu Rev Food Sci Technol. 2015;6:527-57. doi: 10.1146/annurev-food-031414-111800