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| http://dx.doi.org/10.1002/anie.200907235 | DOI Listing |
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Directly probing the heterogeneous conformations of intracellular proteins within their native cellular environment remains a significant challenge in mass spectrometry (MS). Here, we establish an in-cell MS and ultraviolet photodissociation (UVPD) strategy that directly ejects proteins from living cells into a mass spectrometer, followed by 193 nm UVPD for structural analysis. Applying this approach to calmodulin (CaM), we reveal that it adopts more extended conformations within living cells compared with purified samples , highlighting the unique influence of intracellular environments on protein folding.
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Host-guest supramolecular fluorescence probes have garnered significant attention in the detection and sensing of bioactive molecules due to their functionalization potential, adjustable physical properties, and high specificity. However, such probes that reliably, rapidly, and specifically measure neurotransmitter dynamics at the cellular and in vivo level have yet to be reported. Herein, we present a supramolecular fluorescent chemosensor designed for norepinephrine (NE) detection, showing an exceptional response and specificity through host-guest complexation.
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