The summer of 2022 I worked with Dr. Taylor Arhar on studying molecular chaperones, which are proteins that help cells survive stress. We set out to study an interaction between two E. coli chaperones, Dnak (a type of protein called an Hsp70) and CbpA (a type of protein called a J-domain protein of JDP). Hsp70’s help cells survive stress by performing a multitude of functions, the most significant for this study being the folding and re-folding of other proteins, which plays a role in bacterial antibiotic resistance.

While DnaK itself is not necessarily an ideal drug target, it requires cooperation with JDPs such as CbpA to function correctly, so we did work to study how these two proteins interact, in the hopes that one day a drug could be developed to impede this interaction and circumvent antibiotic resistance. While we were not able to study the interaction in the limited time frame, we did succeed in making bacteria overproduce CbpA to study via recombinant protein expression, and purified the expressed CbpA via affinity purification.

Bobby was advised by Taylor Arhar, Assistant Professor of Chemistry

Pakula Biomedical Fellowship Information