Simulation and assay of protein biotinylation with electrochemical technique

Protein biotinylation plays an important role in metabolism and transcription regulation, so study of protein biotinylation has received more and more interests. In this work, the bifunctional Escherichia coli biotin-inducible repressor protein A (BirA) and its substrate for protein biotinylation, a unique peptide with a specific sequence, are introduced as a model to electrochemically simulate the committed step in fatty acid biosynthesis. With the help of gold nanoparticles and peroxidase-labeled streptavidin involved in the electrochemical system, protein biotinylation is achieved on the surface of the working electrode, and the process of protein biotinylation can be electrochemically assayed by the obtained electrochemical response. Therefore, a new method to assay protein biotinylation is proposed and this work may provide a new perspective for understanding protein biotinylation in vitro.