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N-Terminal protein modification using adenosine substrates and aminoacyl transferase
The conjugation of synthetic molecules to the termini of proteins with minimal effects on protein folding and function is an active area of biochemical research. Previous N-terminal protein modification methods suffer from side reaction products, incomplete specificity, low yields, and harsh organic solvent conditions.
Researchers in the Petersson Lab have developed a minimal system for N-terminal protein labeling that uses an adenosine substrate of natural or unnatural amino acids and a single, readily available enzyme, aminoacyl tRNA transferase (AaT) from E. coli.
The use of aminoacyl adenosyl donors increases the substrate scope and reaction scale for N-terminal protein modification. This process gives high yields of modified proteins under nondenaturing conditions to maintain natural protein folding and activity, while requiring only a single basic amino acid for specific recognition. Furthermore, the reaction can be scaled to large quantities of protein because there is no reliance on purified tRNA as with fully enzymatic modification methods.
Transferase-mediated N-terminal protein modification
E. James Petersson, Associate Professor of Chemistry
Stage of Development:
Docket # X5991