The Science Behind Collagen Aktiv.
This section is intended for more explorative minds.
Summary
Collagen Aktiv is a protein present in the skin of freshwater fish which has passed (in its integral and isolated form) through a process of extraction and hydration, from its maternal organism to a water solution which preserves its tertiary triple helical structure. As far as the amino acids composition and its structure (up to the level of tertiary connections) fish collagen is nearly identical to human collagen. It takes the form of a natural gel of high cosmetic value. Thanks to its conformation, Collagen Aktiv displays biological activity. While penetrating the extracellular space of the epidermis, it has an indisputably confirmed influence on the activity of keratinocytes and fibroblasts and brings about a full range of cosmetic and dermatological effects.
Extraction process enables the fish skin proteins to be transformed into a water solution without losing the triple helix conformation in the form of tertiary soluble collagen (tropocollagen). That process, called hydration leaves tertiary collagen molecules intact, as oppose to hydrolysis required to derive collagen from higher grade, insoluble bovine fibers. From the development stage at the level of fibrils (quaternary collagen structure), collagen may not be hydrated (it is insoluble). Hydrolysis (used to obtain collagen for other than GC products) breaks high grade collagen fibrils and fibers into a mixture of inactive peptide fragments and amino acids. Mammalian collagen hydrolysate is nothing more than a bundle of peptides shredded for purpose of dilution, unable to penetrate layers of epidermis and stimulate collagen production.
The fish collagen hydrate obtained in the process of extraction and hydration of the skin proteins retains its triple helical spiral structure outside its natural environment (that is inside a vertebrate organism).
The water soluble fish collagen hydrate in the form of the gel applied onto human skin (due to higher temperature of human body) starts to break its spiral structure stabilized by hydrogen bonds and release smaller peptide chains and amino acids able to penetrate extracellular matrix within the epidermis and dermis layers. Their ability to penetrate skin layers has been known and clinically proven utilizing multiple scientific methods. Upon absorption the full spectrum of naturally sequenced amino acids rapidly enriches extracellular matrix, in one way serving as a “building material” providing components for the collagen production and in the other way creating an environment favorable for keratinocytes to increase the number of cytokines, which in turn stimulate the proliferation of fibroblasts and production of new collagen.