Question

monitor live sirt1 activity using tpe probe: how does it work? the fluorescent probe is non-emissive in aqueous medium. however, the acetyl group of lysine can be deacetylated by sirt1. then the hydrophobic tpe residues aggregate to induce the light-up fluorescence in aqueous solution.

Answer 1

The process you're describing involves monitoring the live activity of SIRT1 (Sirtuin 1), a protein that plays a role in various cellular functions, including gene expression, DNA repair, and metabolism.

The monitoring is done using a fluorescent probe, specifically a tetraphenylethene (TPE) probe.

The TPE probe is initially non-emissive in an aqueous (water-based) medium. This means that it does not emit light in its original state. SIRT1 is known to deacetylate lysine residues on proteins. In this case, the acetyl group of lysine is removed by SIRT1 during its enzymatic activity.

The removal of the acetyl group triggers a change in the TPE probe. The hydrophobic (water-repelling) TPE residues become exposed or induced as a result of the deacetylation process.