The Amazing History of Collagen.

When holding a jar of biologically active collagen in our hands, taking a little of it with a scalded teaspoon, and applying it onto our skin, we hardly ever realize how many years, how much effort, research and experimenting it took to obtain it.

Few realize that the delicate preparation in the jar is practically the very same substance we are built of, the substance we begin to lose faster and faster when we are getting older.

Many people wonder why it is necessary to stick to such strict rules of its storage and application. It is not that easy to comprehend we are holding in our hands “live protein”, which – much as the collagen in our own body – disintegrates due to adverse factors.

In search of lost youth.

Collagen makes up 25 percent of the dry mass of our body and 75 percent of the dry mass of our connective tissue. It would probably win the contest for the most important protein in our body. It is a live frame underpinning the tissues of our various bodily organs. Moreover, it has to be intelligent, able to conform to the demands of different organs as diverse as skin, bones, genitals, kidneys, blood vessels, heart, eyes, or liver. Its structure is even more sophisticated than a DNA particle, containing our genetic code.

Our body synthesizes collagen continuously. Every year ca. 3 kg of our collagen undergoes degradation while another 3 kg is created. It is synthesized from 20 different amino acids into huge chains made up of 1000 amino acid each. It creates gigantic triple helices – complicated spiral conformations each made of three polypeptide chains, whose sophisticated structure resembles a Bach fugue.

There may come a time, however, when we run short of collagen. The process of its renewal may be disturbed either when we lose too much of properly built collagen, e. g. due to disease, stress, UV rays, contact with synthetic chemical substances or other harmful factors, or when its synthesis proceeds too slowly or even stops altogether, which happens when we grow old.

Considering such importance of collagen in our body, it is no wonder that science has long been working on methods of obtaining this protein, which would make it applicable in medicine and cosmetic science.

In the cosmetic science all over the world, “collagen” – obtained usually from cows – has been in use for many decades. Does such “collagen”, however, resemble the collagen which makes up the organs of vertebrates?

In such a figurative sense, bone glue, fried fish or gelatine are also “collagen”, even though they are in fact a result of collagen degeneration. The difference between them and the biologically active collagen is that they are not “alive”. During the process of their production the enormous sophisticated collagen triple helix disintegrates once and for all, unable to regain its previous properties. No one puts grilled salmon on his face in hope to get rid of the wrinkles. Such degenerated “collagen” may turn out to be helpful in some cosmetological applications, still it can by no means compete with “live” biologically active collagen and its role in human body and skin.

The results of the scientific efforts to obtain biologically active collagen, which were pioneered in the 1960s by Paul Börnstein, have been similar to that. Börnstein developed an extraction-based method of obtaining collagen. After many years, however, this outstanding collagen researcher admitted that what he had obtained was not in fact biologically active collagen, but only fragments of its triple helix, being the result of its irrecoverable degradation.

In spite of this, all the later attempts at obtaining collagen were based on extraction. They, however, turned out to be too aggressive to collagen, damaging the delicate bonds of the triple helix. The result of all those methods was, in fact, the products of collagen particle degradation.

Born on the sea

The beginnings of the breakthrough collagen research go back to the 1980s. The scientists from Gdansk – Maria Sadowska, Ilona Kołodziejska, Eugeniusz Krajewski – carried out trailblazing experiments in the field of marine peptide biochemistry. In 1985, Mieczysław Skrodzki, Antoni Michniewicz, and Henryk Kujawa, chemists from the Gdansk Polytechnic, extracted collagen from fish skin. The research continued, the methods were being improved.

Still, the revolutionary method was not yet there.

In the beginning of the 1990s, collagen drew interest of Professor Józef Przybylski Sc.D., biochemist from the Gdansk University. During numerous experiments, which he carried out together with his wife Krystyna Siemaszko-Przybylska, M.D., in order to obtain biologically active collagen, they developed a method of filtration of fish skin collagen through fibroins produced by silkworm (Bombyx mori). Their method preserved the spatial conformation of the precious and frail particles of this protein.

The Przybylskis invention breaks off with methods based on extraction, using process of hydratation instead. Hydratation preserves the delicate bonds of collagen helix and thus makes it possible to obtain tropocollagen – intact collagen, identical with collagen synthesized in the organisms of vertebrates, biologically active. Moreover, the collagen obtained from fish is more noble and safe than collagen obtained from mammals, it also has a better chemical and physical durability.

Thanks to all these efforts by the Polish scientists, methods of collagen production were devised which preserve its unique spatial conformation – triple helix made up of amino acid chains. This is why such collagen can achieve what has been impossible for “collagen” which cosmetic science has used so far. Namely, it can replenish collagen deficits in the organs of the human body.

The biologically active collagen preparations, which for several years have been available on the market, have proved that collagen of this kind makes it possible to certain extent to reverse the effects of ageing. By replenishing the collagen deficits in the dermis, it can both make us look younger and prevent various disfunctions and defects of skin. Since biologically active collagen is too delicate to apply synthetic chemical substances in the process of its manufacturing and storage, it is thus perfectly tolerated even by very sensitive skin. The skin recognizes it as “friendly” and lets it penetrate inside.

AP Ltd. company, being for many years the general distributor of biologically active collagen, manufactured according to the Przybylski method, has gained extensive knowledge and experience concerning both the properties of collagen and the methods of its effective application, which are always adapted to individual needs.

We have decided to offer our Clients the most up-to-date, perfected formula of biologically active collagen AP BIOAKTIV, under the brand ANNA PIKURA. This formula has been developed by eminent specialists in the field – chemists and biochemists.

Since the previous producer of biologically active collagen has lost credibility in the eyes of the Authors of the method, who were denied the possibility of supervising the proces of manufacturing, aware of the needs of the market we have decided to introduce our own product, which would satisfy our Clients’ expectations.

The unique properties of our biologically active collagen are:

1. no preservatives added.

2. high thermal stability, preserving its biological activity even in higher temperatures,

3. still higher biophysical and biochemical similarity to the collagen naturally produced in the human body (by fibroblasts and chondrocites),

4. its composition strictly controlled in the aspect of content of minerals, vitamines and micro- and macroelements which are essential in restoring homeostasis (balance) in the body on cellular level.

Our preparation is an innovative achievement, unprecedented on the market. Its purpose is to restore the functions of healthy body even faster and more efficiently.

We are honored to present to you this unique product of unparalleled qualities, absolutely convinced it will prove to be an indispensable help in deterring the effects of passage of time.