Identified two proteins that "hide" cancer in the immune system

Scientists of the George Mason University (United States) have discovered the exact location of two proteins what are the responsible for hiding cancer cells to the immune system, something that, as they point out, opens new research channels in the development of new drugs to fight cancer.

Thanks to this finding, published in the 'Journal of Biological Chemistry' and collected by, researchers point out that existing intravenous therapies can be replaced by pill-shaped immunotherapy medications.

The discovery has been made thanks to a new technique, known as "protein painting technology". This process begins with two or more proteins that, when joined together, drive the disease. Scientists use small molecule dyes to paint the bound proteins, and then a chemical reaction, known as denaturation, cuts them.

Enhanced Technique

In the last step, scientists use a Mass spectrometer, which allows to determine the distribution of the molecules of a substance based on its mass, to identify the unpainted regions, which is where proteins are touched.

Current technologies in the discovery of drugs at an early stage, such as crystallographyare often complicated, expensive and require a lot of time.

According to the researchers, existing intravenous therapies can be replaced by pill-shaped drugs

Protein painting technology specifically identifies the contact points between proteins, highlighting an ideal location and the recipe to follow for drug development. The technology allows rapid tests of the drug's performance, which means that you can obtain results in several days, instead of in years.

Faster response

In the article, the team of researchers, led Amanda Haymond, describe how they improved this technology, developing and optimizing a new protein dye that has been successfully tested in clinically relevant protein complexes, such as PD-1 and PD-L1.

"The secret to using the protein painting technique is have the perfect dye molecule with the right structure to firmly bind to proteins, "said Haymond.

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