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Amyloid proteins are associated with a broad spectrum of neurodegenerativediseases. However, it remains a grand challenge to extract molecular structureinformation from intracellular amyloid proteins in their native cellularenvironment. To address this challenge, we developed a computational chemicalmicroscope integrating 3D mid-infrared photothermal imaging with fluorescenceimaging, termed Fluorescence-guided Bond-Selective Intensity DiffractionTomography (FBS-IDT). Based on a low-cost and simple optical design, FBS-IDTenables chemical-specific volumetric imaging and 3D site-specific mid-IRfingerprint spectroscopic analysis of tau fibrils, an important type of amyloidprotein aggregates, in their intracellular environment. Label-free volumetricchemical imaging of human cells with/without seeded tau fibrils is demonstratedto show the potential correlation between lipid accumulation and tau aggregateformation. Depth-resolved mid-infrared fingerprint spectroscopy is performed toreveal the protein secondary structure of the intracellular tau fibrils. 3Dvisualization of the \b{eta}-sheet for tau fibril structure is achieved.

Mid-infrared Chemical Imaging of Intracellular Tau Fibrils using Fluorescence-guided Computational Photothermal Microscopy