The Amazing History of Collagen

When holding a bottle of biologically active collagen peptide in our hands we hardly ever consider how many years, how much effort, research and experimentation it took to obtain it.

Few realise that the delicate preparation in the capsules is practically the very same substance we are built of, the substance we begin to lose faster and faster as we get older.

Collagen makes up 25% of the dry mass of our body and 75% 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. It must conform to the demands of different organs, as diverse as skin, bones, ligaments, kidneys, blood vessels, heart, eyes, or liver. Its structure is even more sophisticated than a DNA particle, containing our genetic code.

Our body synthesises collagen continuously. Every year approximately 3 kg of our collagen undergoes degradation while another 3 kg is created. Our body synthesises it from 20 different amino acids into huge chains. It creates gigantic triple helixes. These are complicated spiral conformations, each made of three polypeptide chains. Their sophisticated structure resembles a Bach fugue.

There will come a time, however, when we run short of collagen. Disease, stress, UV rays, contact with synthetic chemical substances, or other harmful factors can disturb the renewal process. The process can also slow naturally as we grow older. After the age of 25, we start to lose collagen from our bodies at a rate of 1.5% per year. By the age of 45, we will have lost up to 30% of our body’s collagen.

Considering the importance of collagen in our body, it is no wonder that science has long worked on methods of obtaining this protein. Researchers wanted to make it effectively applicable in medicine and cosmetic science.

Chase after collagen

For centuries, scientists and beauty therapists have fought to improve the visible effects of ageing on the human complexion. They have searched for ways to reduce facial lines and wrinkles, improve skin elasticity, enhance hair thickness and gloss, and strengthen brittle fingernails to create a more youthful look.

In Traditional Chinese Medicine, people have used Ejiao, made from Donkey-hide Gelatine, since ancient times. People have told many stories about famous figures taking Ejiao.

• Cao Zhi (192-232), the great writer, was unnaturally thin. But he was so invigorated by taking Ejiao that he called it an elixir.

• Yang Yuhuan was one of the four great beauties of ancient China. She lived at the time of the Tang Dynasty (618-907). People said she had the fairest skin of any woman. The poet Xiao Xingzao showed that every day Yang ate soup, made from Ejiao, rice wine, walnuts, black sesame and crystal sugar.

• The Song Dynasty(960-1279) philosopher Zhu Xi once wrote to his mother, advising her to take Ejiao frequently in order to extend her life.

• Li Hongzhang, a minister at the Qing Dynasty (1644-1911) court, travelled to Britain in 1896. He was 74 years old at the time. Throughout the long journey, he took medicines he had brought from the imperial palace, including Ejiao, and returned to China in good health.

In the modern era, cosmetic scientists all over the world use ‘collagen’, though it is usually obtained from cows (bovine). They have been using it for many decades. However, does bovine-extracted collagen really resemble the bioactive triple helixed collagen (tropocollagen) which makes up the organs of living vertebrates?

The search for purity

Paul Börnstein pioneered scientific efforts to obtain biologically active collagen peptide in the 1960s. He developed an extraction-based method of obtaining collagen. After many years, however, this outstanding collagen researcher admitted he had not in fact obtained biologically active collagen. Instead, he had only partial and incomplete fragments of its triple helix, a lacklustre result stemming from irrecoverable degradation in his extraction process.

In spite of this, later researchers still based their attempts at obtaining collagen on an extraction methodology. Yet these processes turned out to be too aggressive to collagen, and damaged the delicate bonds of the triple helix. The result of those methods was yet more examples of collagen particle degradation.

In a figurative sense, people call bone glue, fried fish or gelatine ‘collagen’. However, they are in fact a result of collagen degeneration. The difference between the above and biologically active collagen is that they are not “intact”. During the process of their production the enormous sophisticated collagen triple helix disintegrates once and for all, unable to regain its previous properties. After all, no one puts grilled salmon on their face in the hope of getting rid of wrinkles.

While degenerated “collagen” may turn out to be helpful in some cosmetic applications; it can by no means compete with “intact” biologically active collagen and its role in the human body and skin.

Born on the sea: marine collagen peptide

The beginnings of the breakthrough in collagen research go back to the 1980s. Scientists from Gdansk (Maria Sadowska, Ilona Kolodziejska, Eugeniusz Krajewski) carried out trailblazing experiments in the field of marine peptide biochemistry. In 1985, chemists from the Gdansk Polytechnic (Mieczyslaw Skrodzki, Antoni Michniewicz, and Henryk Kujawa), extracted collagen from fish skin. Their research continued, they improved their methods.

The scientists discovered, and then refined, the method of hydrolysation. Hydrolysation preserves the delicate bonds of the collagen helix. This makes it possible to obtain tropocollagen, or intact collagen, identical to that synthesised in the organisms of vertebrates. Most crucially, the resulting collagen peptide is biologically active, much like the collagen your body produces. Moreover, collagen obtained from fish is safer than collagen obtained from mammals; it also has a better chemical and physical durability.