- Medication targets a specific enzyme that fuels the spread of tumours
- It does this by binding to the membrane of rapidly multiplying cells
- This hijacks cancer’s ‘survival mechanism’ and prevents tumours from thriving
- It is unclear when the drug, which is unnamed, may be available for patients
- Around 357,000 people get diagnosed with cancer every year in the UK
A cancer drug is in development that could stop the disease in its tracks.
The unnamed medication targets a specific enzyme that fuels the spread of tumours, new research reveals.
It does this by binding to the membrane of rapidly multiplying cells, a European study found.
This hijacks cancer’s ‘survival mechanism’ and prevents tumours from attaching to the protein they need to thrive.
Around 357,000 people get diagnosed with cancer every year in the UK.
A cancer drug is in development that could stop the disease in its tracks (stock)
Drug hijacks cancer’s survival mechanism
The anti-cancer drug binds to cancerous cells’ membrane protein, known as dehydroorotate dehydrogenase (DHODH).
The researchers analysed how fats, which are the building blocks of cell membranes, and drugs bind to DHODH.
Study author Dr Erik Marklund, from Uppsala University, said: ‘Our simulations show the enzyme uses a few lipids as anchors in the membrane.
‘When binding to these lipids, a small part of the enzyme folds into an adapter that allows the enzyme to lift its natural substrate [the substance an enzyme acts on] out of the membrane.
‘It seems the drug, since it binds in the same place, takes advantage of the same mechanism.’
Potential for more selective treatments
Study author Sir David Lane, from the Karolinska Institute, in Sweden, added: ‘The study helps to explain why some drugs bind differently to isolated proteins and proteins that are inside cells.
‘By studying the native structures and mechanisms for cancer targets, it may become possible to exploit their most distinct features to design new, more selective therapeutics.’
It is unclear when the drug could be available.
The findings were published in the journal Cell Chemical Biology.