Join us in person or via ZOOM
will speak on:
Towards real time information processing systems based on artificial allosteric proteins
Friday, September 16, 2022, B10L Bertrand H. Snell Hall, 3:30 pm
Abstract: Allosteric regulation of proteins has been referred to as the ‘second secret of life’ as it controls every aspect of information and energy processing in biology. Not surprisingly given the importance of allosteric regulation proteins in biology, construction of artificial allosteric proteins converting one type of biochemical signal into another became a central goal of synthetic biology and protein engineering. We demonstrate the conversion of chosen constitutively active enzymes into peptide-operated synthetic allosteric ON switches by insertion of a peptide binding domain into rationally selected sites. Switches based on light emitting, electrochemically active and antibiotic resistance conferring enzymes required minimal optimization and demonstrated a dynamic response up 7000-fold. The peptidic nature of the regulatory ligand enables incorporation of such synthetic switch modules into higher order sensory architectures. Here, a ligand-mediated increase in proximity of the allosteric switch and the engineered activator peptide modulates biosensor activity. We constructed a range of signaling circuits with tunable input and output parameters that quantitatively convert one type of signal into another. To demonstrate the utility of the developed system we constructed sensory bio-electrodes that are able to convert analyte binding into electric current.
