Protein phase separation plays an important role in many biological processes such as cell cycle regulation, transcription regulation, and apoptosis, which is closely associated with the occurrence and development of various human diseases (such as cancers). At present, due to the lack of effective quantitative analysis methods for intracellular protein phase separation, we know little about the spatio-temporal regulation mechanism of intracellular phase separation, which will seriously affect the research progress of protein phase separation and the development of clinical drugs. In this work, taking CRD-BP protein as a model, we determined the phase transition concentration of CRD-BP in solution, and dynamically observed the effects of salt concentration and molecular crowding agent on the phase separation of CRD-BP by fluorescence correlation spectroscopy (FCS). Furthermore, we have established a multi-channel single molecule FCS method for <i>in Situ</i> study of protein phase separation in living cells, which provides a new method for the basic research of protein phase separation, the research of cancer pathology and the screening of drugs.

Study of phase separation in living cells by multi-channel single molecule fluorescence correlation spectroscopy

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