The word collagen is derived from the Greek word meaning glue. The protein collagen is the main substance of connective tissue and is present in all multi-cellular organisms. It is found in many different tissues and organs and its main function is mechanical reinforcement of connective tissues. Collagen also plays a regulating role in developing tissues, influencing the proliferation and differentiation of unspecialized cells.

Collagen is a highly conserved protein preserving the amino acid sequence and typical triple helix structure across species lines. Its unique physico-chemical properties together with its weak immunogenicity in humans and flexible efficacy attributes are appropriate for diverse medical device applications. Thus, for decades, collagen has been extensively used as a biomaterial, safely and effectively, in a variety of medical and surgical procedures.

The major natural mechanism of extending biological half life of the native collagen is glycation induced cross-linking. It is a non-enzymatic reaction, in which sugars in the body, mainly glucose, act as reducing agents to cross link native collagen. Over time, the initial products of this reaction slowly undergo further re-arrangements, resulting in the irreversible formation of a family of cross-linked structures. These structures are ultimately responsible for stiffness of the tissues.