A new research breakdown of protein dinamics could lead to new cancer therapies

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Researchers from Northumbria University in Newcastle, and Bogazici University in Turkey, have found a new way to study the structure and molecular dynamics of single proteins inside the human body – which scientists could help understand the progression and possible treatment of diseases such as cancer.

The team, led by Dr. Hamdi Torun of the Northumbria Department of Mathematics, Physics and Electrical Engineering, a method called the atomic force microscope that allowed them to identify a single protein molecule within a sample of millions and study how it behaved with other molecules.

They combined this method with a computer study led by Professor Turkan Haliloglu, which allows scientists to develop models and model-based data – in this case predicting how molecules might respond and movement after biochemical changes and how this may affect disease progression. .

By being able to identify such lesions, scientists would gain an understanding of mutations-led diseases such as cancer and cystic fibrosis, as well as design more effective drugs to treat or vaccinate against these diseases, and even COVID-19 future.

Commenting on the research, Dr Torun said: “This is the first time that these two methods of experimental analysis and computer analysis have been combined to study specific protein molecules.

“It is not common practice to separate one particular molecule in this way, but the most effective way is to study the structure of the molecule and ask questions such as‘ what if I change a particular part of the protein? ‘or’ what if I bind a particular enzyme to the protein? ‘

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“The answers to these questions allow us to design new drugs to treat diseases such as cancer, which can make a huge difference in people’s lives.”

The research was published in the Iris Biophysical in a paper titled “Oncogenic Mutations on Rac1 Affect Global Sexual Dynamics Underlying GTP and PAK1 Binding.”

An image showing the results of their computer study was also selected to appear on the front cover of the journal (volume 120, issue 5).

The research project, entitled Force and Function in Biological Macromolecules: Molecular Simulation and Single-Molecule Studies, was funded by the Turkish Scientific and Technological Research Council (TUBİTAK).

Commenting on the potential for wider use of this method, Dr Torun said: “For this study we chose to study proteins found in all human cells, but this method could be applied to any protein, for example the spike protein found in Corona-virus.

“This research has great potential to be applied, and we hope it will lead to new developments in disease management in the future.”