Treatment of cancer using the

Scientists have discovered how to destroy cancer proteins that cause many diseases. A Dundee University team has devised a technique called "kiss of the god of death" to destroy this dangerous disease.

Methods for binding molecules to tumors, to spread Ras and Myc proteins. At this point, this is the most promising breakthrough in the fight against cancer.

The lead researcher, Professor Alessio Ciulli, said: "We found that it is important not to have enough neutral protein to place next to harmful proteins. Proteins like Ras and Myc must be directly connected to harmful proteins or "kiss" it In this method, "death kiss" is the key to ensuring the degradation of harmful proteins ".

Ras and Myc are known to cause cancer in humans, and Huntingtin - causes Huntingdon disease (progressive degenerative disease caused by nerve cells in the brain). However, they are still resistant to all drugs so far. Currently, a research group led by Professor Ciulli of the Department of Life Sciences in Dundee has found a way to overcome this.

In the field of cancer research and treatment, this method is not normal. It uses small molecules to target harmful proteins by attaching them to neutralizers. From there start the process of decomposing harmful proteins and thus remove them completely.

New technology helps treat cancer.(Photo: University of Dundee).

Professor Ciulli said: "We know there are many active proteins that cause cancer but we can't prevent this from happening. The main problem is that we can't find small molecules that can bind. success with these proteins and at the same time hinder their function ".

"This is a very complicated area. The proteins can make fake adjustments in the cell and are extremely difficult to inhibit. Our lab research in recent years has contributed to a new approach has been theorized for many years but thanks to recent research they are fully recognized ".

"Instead of using small molecules to try and disable harmful proteins, we have developed a new way to modify. This method is used to attract neutral proteins, bind them to proteins. harmful and against them, from there began a process of recession, " Professor Ciulli added.

Professor Ciulli and colleagues focused their attention on a chemical breakdown molecule called PROTAC (Proteosysis-targeting chimer molecules).

The researchers created the first X-ray crystal structure of a PROTAC - linked to both harmful and neutral proteins. They found that it could be used as a magnet to attach two target proteins together.

Professor Ciulli said: "This discovery provides the first insights into how PROTAC works and how we can decompose target proteins in a selective way?"

"This represents a paradigm shift in selective chemical interventions for proteins. These proteins cause disease but so far we have not been able to find a cure. It is like a something that can't be pierced. "

The work of Dundee group is focused on pairing one of BET's bromodomain proteins, BRD4 - this is a targeted drug for cancer treatment - with a degenerate BRD4 called MZ1 .

They discovered that MZ1 can pull two proteins together by the way the MZ1 folds itself. Once these two proteins are combined in the interactive "kiss" will lead to the target degradation.

Similar proteins BRD2 and BRD3 also do not interact with neutral proteins. Because of this, researchers can design new decomposers without these proteins in the process of decomposition.

This result is important because it explains how decomposing molecules can be designed in the future? And that design is to minimize the target deviation effects, and unlike the use of conventional inhibitors.

Professor Ciulli said there were promising signs from the pharmaceutical industry about investing in this field of research.

"Now we have a better understanding of how to turn inhibitors into decomposers. The way to convert decomposers into drugs will be difficult and we cannot go it alone. It is interesting. When I saw the pharmaceutical industry have made serious commitments, we can be optimistic about this, " said Professor Ciulli.

All research results have been published in Nature Chemical Biology.