Resolving protein condensates and aggregates in vivo by boxcar-enhanced Fluorescence-detected mid-Infrared photothermaL Microscopy (FILM).

Bethany Weinberg, Zhongyue Guo, Rong Tang, Jianpeng Ao, Jiaze Yin, Guangrui Ding, Todd A Blute, Marzia Savini, Giulio Chiesa, Wentao Wang, Matt Good, Meng C Wang, Ji-Xin Cheng

Department of Molecular Biology, Cell Biology, & Biochemistry, Boston University, Boston, MA, USA. · pubmed

Paper

Abstract

Protein assemblies, including aggregates and condensates, are closely linked to health and diseases. We demonstrate boxcar-enhanced Fluorescence-detected mid-Infrared photothermaL Microscopy (FILM), using two model species, Caenorhabditis elegans and Saccharomyces cerevisiae, to quantitatively resolve these protein states in vivo by imaging β-sheet and α-helix secondary structures and analyzing their ratios. This method directly distinguishes polyglutamine (PolyQ) protein aggregates, α-synuclein protein condensates, and P-granule condensates implicated in neurodegenerative diseases and embryonic development in live organisms. It further enables the unraveling of protein assembly dynamics and their physio-pathological roles, such as age-related progression of PolyQ from condensates to aggregates.

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Research summary

The paper claims to quantitatively resolve protein states in vivo, distinguishing between aggregates and condensates linked to neurodegenerative diseases. The research addresses the dynamics of protein assemblies, which are crucial in understanding age-related progression and the underlying mechanisms of diseases associated with aging.

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