Poster Presentation The 44th Lorne Conference on Protein Structure and Function 2019

A Maleimide-functionalized Tetraphenylethene Structural Analog for Measuring Protein Unfolding in Cells (#138)

Oscar Dr Liu 1 , Shouxiang Mr Zhang 1
  1. Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC, Australia

Proteostasis is an important biological event that regulates protein synthesis, folding and degradation1. We previously reported that an aggregation-induced emission (AIE) luminogen, TPE-MI2, which can be used as a great tool to quantify proteostasis imbalance by luminescence upon conjugation with exposed cysteine thiols. Upon structural optimization, we have created a series of TPE-MI analogues with better spectral properties while remaining minimal cytotoxicity, compared to TPE-MI. In this poster, I will present the applications of these probes for reporting on proteostatic stress in cells.

  1. 1.Burslem, G. M.; Crews, C. M., Small-Molecule Modulation of Protein Homeostasis. Chemical reviews 2017, 117 (17), 11269-11301. 2.Chen, M. Z.; Moily, N. S.; Bridgford, J. L.; Wood, R. J.; Radwan, M.; Smith, T. A.; Song, Z.; Tang, B. Z.; Tilley, L.; Xu, X.; Reid, G. E.; Pouladi, M. A.; Hong, Y.; Hatters, D. M., A thiol probe for measuring unfolded protein load and proteostasis in cells. Nature communications 2017, 8 (1), 474.