Rational design of a photo-crosslinking BODIPY for in situ protein labeling

Chem Commun (Camb). 2015 Apr 18;51(30):6643-6. doi: 10.1039/c5cc01068c.

Abstract

Photo-crosslinking agents have emerged as critical tools to investigate protein-protein interactions in complex proteomes, but there are few photocrosslinkers available at the moment. Here, we report the first rational design of a photo-crosslinking BODIPY fluorophore (pcBD) and its biological application for biomolecule labeling. As a photosensitizing functional motif, an aryl ketone group was incorporated into the BODIPY fluorophore, and a series of proteins were labeled by pcBD compounds upon UV irradiation. In order to investigate protein-protein interactions in a protein mixture, amino-functionalized pcBD was prepared and covalently attached to a ubiquitin ligase binding peptide. Upon UV irradiation, we could successfully visualize the substrates in the total lysate. These results provided a proof of concept for spatially controllable tagging via photo-activation of the pcBD scaffold, and demonstrated its potential usage for in situ labeling applications.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Boron Compounds / chemistry*
  • Cross-Linking Reagents / chemistry*
  • Drug Design*
  • Fluorescent Dyes / chemistry*
  • HEK293 Cells
  • Humans
  • Photochemical Processes*
  • Staining and Labeling
  • Ubiquitin-Protein Ligases / chemistry*

Substances

  • 4,4-difluoro-4-bora-3a,4a-diaza-s-indacene
  • Boron Compounds
  • Cross-Linking Reagents
  • Fluorescent Dyes
  • Ubiquitin-Protein Ligases