Separation of Short Fluorescently Labeled Peptides by Gel Electrophoresis for an In Vitro Translation Study

The development of simple, readily available, and sensitive methods for studying bacterial protein synthesis is an important fundamental and applied task. We recently demonstrated the possibility of visualizing short BODIPY-labeled phenylalanine- and leucine-containing peptides using urea-polyacrylamide gel electrophoresis under denaturing conditions. In this work, we expand the range of test sequences and included peptides with valine, lysine, and the modified amino acid epsilon NH2-DOTA-lysine. The described method can also be used to study the mechanism of translation inhibition, as shown by elaboration of the specific action of the antibiotics etamycin A and viomycin.