Editor’s note: This is an excellent “family” of drug molecules with a deep foundation.
In the past hundred years, “talents” have emerged in large numbers among family members, leading the way in clinical application and saving countless lives. You may not know which molecular family they belong to, but you must know their names like penicillin and insulin.
Back in 1901, Professor Emil Fischer, a Nobel Prize winner in chemistry, introduced to the academic community a product molecule from the hydrolysis experiment. The molecule is linked by two glycines, a natural amino acid, through amide bonds. The next year, he gave the molecule a name, peptide, from Pepsis, meaning “degradation products of proteins.”. Since then, peptide molecules have a name of their own, and peptide drugs also opened their own era prologue.
Obviously, the name of the peptide implies its structure, and the peptide can come from the hydrolysis of protein.
Similar to protein, the basic structure of polypeptide is also amino acid; unlike protein, the amount of amino acid in polypeptide is much less than that in protein. Protein molecules are made up of thousands of amino acid molecules. Generally, 2-100 amino acid molecules linked by amide bond (- CONH -) are classified as peptides. The amide bond connecting amino acid molecules is also called peptide bond.
Peptide drug molecules are widely used in clinical practice and are closely related to our health. However, compared with amino acids or proteins, polypeptides may still be a very strange concept for many people. Peptide drugs are not rare, but many times, people don’t know that the drugs to save their lives are just polypeptide molecules.
From life, save life
Different from many drug molecules developed by human beings in time-consuming and laborious search for targets, peptide drugs often exist naturally in nature and regulate various cell behaviors in the body. They come from life itself and are natural drug choices. As the natural starting point of drug development, peptide drug development has great potential and advantages, as long as you have a pair of eyes good at discovering.
There is a very popular story. In 1928, Professor Alexander Fleming, from England, happened to observe a “war” in the microbial community on a culture dish infected with mold. Around the blue mold, the original wanton growth of Staphylococcus aureus position lost, each time “close combat”, Staphylococcus aureus will “retreat.”.
Professor Fleming, who has been exploring the field of anti infection for many years, is keenly aware that there is an anti infective substance in mold. Later, the substance was purified from the mold, and its name was penicillin, the classic anti infective drug, penicillin.
As we all know, penicillin saved many lives in the Second World War, and opened a brilliant era of peptide antibiotics. Generally, penicillin is regarded as a small molecule drug, but little known is that there is a typical peptide bond in the molecular structure of penicillin, which is a dipeptide analogue.
Penicillin has become a very successful antibiotic drug because of its unique mechanism of action. Penicillin inhibits the key enzyme reaction of bacterial cell wall synthesis. However, animal cells have no cell wall. Therefore, penicillin has no high toxicity to human normal cell function while inhibiting bacterial growth. There are many natural peptide drugs like penicillin. Taking endogenous peptide drugs as an example, insulin, oxytocin, calcitonin and somatostatin are widely used in clinical practice.
Blue out of blue
With the development of life science, scientists have gradually realized that many highly active molecules in life are peptides, such as hormones and neurotransmitters, which play a role in regulating the physiological functions of the body.
Although the activity is very high, the natural peptide molecules are easy to be degraded, and the half-life in vivo is short, and it is often damaged by oral administration. Taking insulin as an example, for a long time in the past, peptide drugs mainly rely on clinical injection, and the action cycle is very short, which is a great challenge for patients’ compliance and wide application.
How can polypeptide drugs play a better role in clinical practice? To this end, scientists continue to explore.
Based on the natural molecular structure and artificial modification, polypeptide molecules can be “blue out of blue”.
Using special amino acids to replace the original natural amino acids, or coupling or modifying with larger molecules, combined with the technological breakthroughs in preparation, scientists began to try to optimize the natural peptides in multiple ways, so as to avoid rapid degradation by enzymes, prolong the half-life of peptides, change the administration mode of peptide drugs, and improve the comfort and compliance of patients taking drugs To achieve better therapeutic effect. Nowadays, many artificially optimized insulin analogues have replaced the natural insulin molecules in clinical treatment.
How to reduce R & D barriers?
In many cases, small molecules are easy to produce high cytotoxicity, and the targets for easy preparation of drugs already exist. Macromolecules such as drugs and proteins are easy to produce immunogenicity. Peptide molecules between small molecules and large molecules, with their natural regulatory ability, specificity and wide range of action targets, have increasingly attracted the attention of innovators and investors in the field of new drug development favor.
Peptide drugs are mainly chemical synthesis, but different from small molecules and macromolecules, peptide synthesis needs unique supporting facilities and equipment. For drug research and developers, entering the field of polypeptide means that it may be necessary to build a high infrastructure for peptide drug production from scratch. Time, space, cost and talents are all challenges. In addition, many polypeptide molecules are highly active molecules, which requires very high R & D and production facilities.
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