Newswise — Researchers working with Michael L. Gross, professor of chemistry in Arts & Sciences at Washington University in St. Louis and of immunology and internal medicine at the School of Medicine, and Weikai Li, associate professor of biochemistry and molecular biophysics at the School of Medicine, have developed a novel technique for footprinting integral membrane proteins in lipsosomes, common delivery vehicles for pharmaceutical drugs, including mRNA vaccines.
The new approach forges an important connection between materials science and biology and promises applications in drug design, binding and screening. The research was published in Nature Communications and was recently selected as an editor’s highlight among papers in structural biology, biochemistry and biophysics.
“Membrane proteins are of high importance because they participate in almost all physiological processes and represent more than 60% of drug targets,” Gross explained. “However, there are known structures of only a few hundred of these proteins compared to tens of thousands of structures for soluble proteins, which can be found in water and biological fluids. Thus, there is a large gap to be filled with new footprinting methods focused on membrane proteins.”
Footprinting uses fast chemical reactions to mark the surfaces of proteins and report on the location of amino acids. By combining footprinting with mass spectrometry, researchers can map the location of these chemical markers and observe how protein structure changes under certain conditions. Membrane proteins, as opposed to soluble proteins, have historically been challenging to mark in chemical reactions and to analyze by mass spectrometry.
Read more from Washington University's department of chemistry here:
https://chemistry.wustl.edu/news/chemists-develop-new-footprinting-technique-proteins-living-systems
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