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In the other mode, the probe assesses the polarity. Polar environments indicate an unbalanced electronic distribution, which can be measured by the dielectric constant. To measure this parameter, the researchers added an electronic “push–pull” chemical group to the fluorogenic probe. They observed that, in polar solutions with a high dielectric constant, the fluorogenic probe called NTPAN-MI emitted its fluorescence signal with a color shift. This “chameleon-like” color change thus indicates a polarity change.
The authors tested the NTPAN-MI probe on a human cell line, which they stressed by adding drugs that interfered with protein synthesis and folding. The scientists observed normal fluorescence in untreated cells, but bright fluorescence when unfolded or misfolded proteins accumulated in cells treated with toxins or infected by virus. In addition, the color shift signaled the polarity of the environment and thus the proteome state of each cellular compartment. The researchers reported that they visualized the “unfolded protein load” in the nucleus for the first time. Previous methods could only measure unfolded proteins in the cytoplasm.
With its two sensing modes—measuring unfolding and the polarity of the protein environment—the NTPAN-MI probe provides a sharper picture of the stress responses of live cells than what can be obtained with only one-modal probes or different methods. The authors point out that their method would allow scientists to obtain more accurate knowledge of the crosstalk of the cellular components in response to stress. Source:
Wiley Journal reference:
Owyong, T. C., et al. (2019) A Molecular Chameleon for Mapping Subcellular Polarity in an Unfolded Proteome Environment. Angewandte Chemie International Edition . doi.org/10.1002/anie.201914263 .
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