About Collagen

Representing 60% of the body’s dry weight, collagen is part of all connective tissue, from the membranes of the eyes, to the fibrous material of the bones. Collagen has a variety of functions, such as, for example, helping cell activity and providing an organization matrix for the skin. There are 29 types of collagen. The most common type is Type I Collagen, which is part of the skin, tendons and bones.

WHAT MAKES COLLAGEN TYPE I ESSENTIAL IN THE WOUND HEALING PROCESS?

Type I collagen is necessary for the management of wounds, because it acts as a material that keeps wounds moist, absorbing exudate from them. It has been demonstrated that intact Type I Collagen binds to several proteases and inflammatory cytokines that are in excess in exudates from chronic wounds, including neutrophil elastase, MMP-2, Interleukin IL -6, IL-8 and IL-1β.

In addition, collagen provides a matrix for cell growth, leads to a significant increase in the number of fibroblasts, increases the deposition of guided and organized collagen fibers, assists in the assimilation and bioavailability of fibronectin, helps maintain the chemical microenvironment and thermostatic wound, and inhibits or deactivates excessive matrix metalloproteinases.

WHAT SOURCES OF COLLAGEN ARE MOST SUITABLE FOR THE TREATMENT OF WOUNDS?

The sequence of the amino acids chain in bovine collagen is very similar to the sequence of human collagen. In fact, the genetic difference between bovine and human collagen is only 5%. Because of this similarity, bovine collagen is unlikely to cause an allergic response in humans.

NOT ALL COLLAGEN THAT IS PRODUCED IS EQUAL

CHEMISTRY AND STRUCTURE: Collagen has a chemical structure that allows it to absorb large amounts of exudate. It is important to preserve the chemical and structural characteristics of collagen. Certain products that are on the market, such as denatured or hydrolyzate collagen, have had their original molecular structure altered. These altered collagen products have been designed to offer certain benefits, but, at the same time, lose certain beneficial properties of natural collagen. As seen in the figure below, the altered collagen lacks the non-helical domains, producing disorganized fibers  or a disordered matrix. On the other hand, the fibers of natural collagen, self-assemble into aggregates resembling the structure of a rope.