The folding state of the proteins in live cells often reflect the cell’s general health. Australian scientists have developed a molecular probe that senses the state of the proteome — the entire set of the proteins — by measuring the polarity of the protein environment. The fluorescence signal of the probe quantifies unfolding and its chameleon-like color shift maps the cellular regions of enhanced misfolding, says the study published in the journal Angewandte Chemie.
If live cells are stressed, protein-synthesis and folding-correction mechanisms are out of balance. Misfolded proteins remain stuck, enhanced degradation occurs, and inactive proteins and protein debris aggregate to form granules and condensates in the cytoplasm. Such aggregates play an important role in neurodegenerative diseases and cancer. One driving factor for the aggregation of misfolded proteins seems to be the polarity — the electronic distribution in an environment. Yuning Hong and colleagues at La Trobe University Melbourne and The University of Melbourne, Australia, have designed a two-modal fluorogenic probe to monitor protein aggregation in greater detail.
