The Swiss Federal Institute of technology in Lausanne, scientists first synthesized an amino acid that can shape the structure of active peptides and enhance its efficacy. The experiment showed that the amino acid can be increased by more than 40 times when it was inserted into biologically active peptides. With this result, a series of new drugs are expected to be developed. Related papers published in the journal Nature chemistry.

At present, the drugs used in our country are mainly made of two kinds of substances, one is a naturally occurring polypeptide substance, and the other is a protein. Although there are many kinds of peptides and proteins, there are only 20 kinds of natural amino acids. Each amino acid has different structure and chemical properties, and the combination of different amino acids has produced various features and functions of peptides and proteins.

Until recently, the vast majority of amino acid based drugs are also used in the original nature of the amino acids, such as hormones, insulin, antibiotics, cyclosporine, etc.. However, the emergence of a variety of new diseases and the evolution of the original bacteria, viruses, scientists need to develop new, more effective drugs. One way to meet this demand is directed evolution, that is, to simulate the development of nature in the laboratory and to develop new peptides and proteins.

According to physicist organizational network September 1st (Beijing time) reported that the Federal Institute of technology in Lausanne, Christian Hines led the research team developed a synthesis of amino acids, its unique structure can significantly improve the therapeutic efficacy of peptides and proteins. This synthetic amino acid is very similar to a natural amino acid known as cysteine. Cysteine contains other natural amino acids do not have sulfur group, which makes it possible to combine with another cysteine to form a new structure, thereby affecting the function of peptides and proteins.

The researchers first designed 5 similar amino acid cysteine, and integrate it into the structure of two kinds of bioactive peptides, one can inhibit enzymes associated with cancer, one can block the neuronal receptors found. Tests show that compared with traditional drugs, the new drug activity is nearly 40 times higher.

Hayes said: "this is very surprising. Normally, if you touch the natural molecules, you can only make things worse. In this case, we find that on the contrary, we get the desired results. In the study, we learned that the diversity of the peptide library structure is the key to achieving a good combination and better results. With this new amino acid, a highly diverse peptide structure can be produced."

Bicyclic peptides have been thought to be able to replace small molecules or antibodies used in common drugs for the treatment of diseases. The new therapeutic peptides will play an important role in drug design in the future. Hayes said that they have developed the use of bicyclic peptides to develop drugs for the treatment of a variety of diseases, the next step will be the use of this new amino acid directed evolution experiments.