Fighting cancer effectively often involves stopping cancer cells from multiplying, which requires understanding the proteins that the cells rely on to survive. Protein profiling plays a critical role in this process by helping researchers identify proteins-; and their specific parts-; that future drugs should target. But when used on their own, past approaches haven't been detailed enough to spotlight all potential protein targets, leading to some being missed.
Now, by combining two methods of protein analysis, a team of chemists at Scripps Research has mapped more than 300 small molecule-reactive cancer proteins, as well as their small molecule binding sites. Revealing key protein targets that, when disrupted with certain chemical compounds (or small molecules), halt cancer cell growth may eventually enable the development of more effective and precise cancer treatments. The findings were published in Nature Chemistry on August 13, 2024.
One method gave us a broad view of which proteins were interacting with the chemicals, and the second method showed exactly where those interactions were happening." Benjamin Cravatt, PhD, Study Co-Senior Author and Norton B. Gilula Chair in Biology and Chemistry, Scripps Research Institute Both methods are forms of activity-based protein profiling (ABPP), a technique that Cravatt pioneered to capture protein activity on a global scale.
The research team used their dual approach to flag both the proteins and protein sites that interacted wit.