West Virginia University researchers mapped the crystal structure of the protein and located how a drug fixes on it.
Researchers revealed how medications are attached to the proteins in our body, how they work and what form they acquire.
They mapped the crystal structure of a protein in our cells and determined how a drug latches onto it.
The research is funded by the West Virginia Clinical and Transitional Science Institute focused on the protein called mitoNEET.
The mitoNEET inhabits the outer membrane of our mitochondria, which act like power plants that energise our cells.
The researchers isolated mitoNEET from both bacterial overexpression and animal models exposed synthesised 11 molecules similar to furosemide which is a common diuretic sold under the brand name LASIX.
After the molecules bonded to the mitoNEET, the researchers built atom-by-atom mapping the pairings. They remotely controlled samples with ultra-bright, high-energy X-rays to reveal how precisely molecules come together.
The team discovered that the molecules docked into a cluster of iron and sulfur atoms that made up part of the protein.
The understanding of cellular function could improve the performance of drugs that work by altering the protein’s activity.
For example, adding an extra oxygen group to a drug’s molecular structure could dramatically tighten its bond to mitoNEET and eliminate unintended binding to other cellular proteins.
