Scientists are coming up with diverse possible methods to examine complex proteins. Yes, Rice University chemists have crafted a synthetic enzyme that could assist in revealing the identities of several difficult-to-study proteins, counting many that seemingly play vital functions in cancer and other disease. The co-author of the study is Zachary Ball, assistant professor of chemistry at Rice.
Ball started investigating dirhodium catalysts more than three years ago. The expert was captivated by a study that presumably exhibited dirhodium catalysts could be used to alter tryptophan, one of the 21 amino acids that are said to be the fundamental building blocks of life.
Zachary Ball commented, “We have combined the chemical capabilities of rhodium with what biology already knows about recognizing and selecting specific proteins. The result is a tool that, in many ways, is more powerful than any biological or chemical approach alone.”
Catalysts improve chemical responses by augmenting the rate of reaction without being consumed themselves. In living things, proteins known as enzymes seemingly serve the same purpose. But unlike several inorganic catalysts, enzymes are believed to be rather choosy. In a procedure that biologists often associate to a ‘lock and key’, enzymes connect to only those molecules that correspond to their shape precisely. This may avert them from inciting irrelevant reactions all through the cell.
Ball and postdoctoral research associate Brian Popp pondered if they could get the selectivity of enzymatic reactions marry a rhodium-based catalyst. They examined the notion by binding their channel to a small segment of protein that may drape with other proteins. This ‘coiled coil’ wrapping motif is believed to be general in biology, predominantly in signaling proteins. Signaling proteins are seemingly those that trigger or deactivate key processes such as apoptosis, the ‘programmed death’ response that’s identified to play a vital function in cancer.
Ball mentioned, “Signaling pathways are like a trail of dominos. Dozens of proteins can be involved, and they interact one after the other in a cascade. In most cases, the interactions are both fleeting and weak. They are difficult to observe with traditional methods, and as a result we are still in the dark about the roles that key signaling proteins play in health and disease.”
Ball mentioned that his and Popp’s synthetic enzyme strategy could aid in cracking that issue. In their tests, the chemists could create synthetic enzymes that may selectively connect with proteins and fasten tags that would enable biologists to recognize them.
Apart from tryptophan, the technique worked with phenylalanine and tyrosine, two amino acids usually seen in signaling proteins. And new unpublished studies point out the researchers’ approach could function for even more amino acids.
Ball mentioned that the process ought to be refined before it could be applied in most of the biology labs, but he and Popp are already working toward understanding extensive applications of the strategy.
The study was published in the Journal of the American Chemical Society.