Boston College researchers used a mild charge of electricity to precisely modify proteins, a new tool that can be used to develop novel biotherapeutics and protein-based research tools, the team reported recently in the journal Nature Chemistry.
Identifying a specific site for protein modification is challenging due to the complexity of proteins made from 20 amino acids, making achieving site-specificity difficult. To overcome challenges, the team sought to develop a method to incorporate a non-natural amino acid at any chosen site(s) of a protein. The team accomplished this by reengineering the translation system of cells to accommodate the new amino acid 5-hydroxytryptophan (5HTP).
Typically, researchers start with small molecules, in this case 5HTP and aniline, then move on to large proteins. But first attempts at the reaction between 5HTP and anilines at the small-molecule level was messy, as the 5HTP molecules reacted preferentially with each other. But when 5HTP was incorporated into a large protein, it was no longer able to react with another protein-bound 5HTP, and cleanly reacted with an aniline instead, the team reported.
Thus the team, led by BC professors of chemistry Abhishek Chatterjee and Eranthie Weerapana, developed and optimized a novel electrochemical protein labeling reaction called "eCLIC", that enables precise modification of site-specifically incorporated 5HTP residues on many different proteins including full-length therapeutic antibodies.
From: EurekAlert!
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