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<p>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, <i>Caenorhabditis elegans</i> and <i>Saccharomyces cerevisiae</i>, 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.</p><p></p>

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

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年5月11日

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  • 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

摘要

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.