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Jun 15, 2023;12 (1): 147.

Mid-infrared chemical imaging of intracellular tau fibrils using fluorescence-guided computational photothermal microscopy.

Jian Zhao, Lulu Jiang, Alex Matlock, Yihong Xu, Jiabei Zhu, Hongbo Zhu, Lei Tian, Benjamin Wolozin, Ji-Xin Cheng
Author Information
  1. Jian Zhao: Department of Electrical and Computer Engineering, Boston University, Boston, MA, 02215, USA. jianzhao@knights.ucf.edu. ORCID
  2. Lulu Jiang: Department of Pharmacology and Experimental Therapeutics, Boston University School of Medicine, Boston, MA, 02118, USA.
  3. Alex Matlock: Department of Electrical and Computer Engineering, Boston University, Boston, MA, 02215, USA. ORCID
  4. Yihong Xu: Department of Physics, Boston University, Boston, MA, 02215, USA.
  5. Jiabei Zhu: Department of Electrical and Computer Engineering, Boston University, Boston, MA, 02215, USA.
  6. Hongbo Zhu: State Key Laboratory of Luminescence and Applications, Changchun Institute of Optics, Fine Mechanics and Physics, Chinese Academy of Sciences, 130033, Changchun, China. ORCID
  7. Lei Tian: Department of Electrical and Computer Engineering, Boston University, Boston, MA, 02215, USA. ORCID
  8. Benjamin Wolozin: Department of Pharmacology and Experimental Therapeutics, Boston University School of Medicine, Boston, MA, 02118, USA.
  9. Ji-Xin Cheng: Department of Electrical and Computer Engineering, Boston University, Boston, MA, 02215, USA. jxcheng@bu.edu. ORCID
PMID: 37322011 DOI: 10.1038/s41377-023-01191-6

Abstract

Amyloid proteins are associated with a broad spectrum of neurodegenerative diseases. However, it remains a grand challenge to extract molecular structure information from intracellular amyloid proteins in their native cellular environment. To address this challenge, we developed a computational chemical microscope integrating 3D mid-infrared photothermal imaging with fluorescence imaging, termed Fluorescence-guided Bond-Selective Intensity Diffraction Tomography (FBS-IDT). Based on a low-cost and simple optical design, FBS-IDT enables chemical-specific volumetric imaging and 3D site-specific mid-IR fingerprint spectroscopic analysis of tau fibrils, an important type of amyloid protein aggregates, in their intracellular environment. Label-free volumetric chemical imaging of human cells with/without seeded tau fibrils is demonstrated to show the potential correlation between lipid accumulation and tau aggregate formation. Depth-resolved mid-infrared fingerprint spectroscopy is performed to reveal the protein secondary structure of the intracellular tau fibrils. 3D visualization of the β-sheet for tau fibril structure is achieved.

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Grants

  1. P41 EB031772/NIBIB NIH HHS
  2. R35 GM136223/NIGMS NIH HHS
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