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Self-driving microscopy detects the onset of protein aggregation and enables intelligent Brillouin imaging

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  • Khalid A. Ibrahim

    (École Polytechnique Fédérale de Lausanne (EPFL)
    École Polytechnique Fédérale de Lausanne (EPFL)
    École Polytechnique Fédérale de Lausanne (EPFL))

  • Camille Cathala

    (École Polytechnique Fédérale de Lausanne (EPFL))

  • Carlo Bevilacqua

    (European Molecular Biology Laboratory (EMBL))

  • Lely Feletti

    (École Polytechnique Fédérale de Lausanne (EPFL)
    École Polytechnique Fédérale de Lausanne (EPFL))

  • Robert Prevedel

    (European Molecular Biology Laboratory (EMBL)
    German Center for Lung Research (DZL))

  • Hilal A. Lashuel

    (École Polytechnique Fédérale de Lausanne (EPFL))

  • Aleksandra Radenovic

    (École Polytechnique Fédérale de Lausanne (EPFL)
    École Polytechnique Fédérale de Lausanne (EPFL))

Abstract

The process of protein aggregation, central to neurodegenerative diseases like Huntington’s, is challenging to study due to its unpredictable nature and relatively rapid kinetics. Understanding its biomechanics is crucial for unraveling its role in disease progression and cellular toxicity. Brillouin microscopy offers unique advantages for studying biomechanical properties, yet is limited by slow imaging speed, complicating its use for rapid and dynamic processes like protein aggregation. To overcome these limitations, we developed a self-driving microscope that uses deep learning to predict the onset of aggregation from a single fluorescence image of soluble protein, achieving 91% accuracy. The system triggers optimized multimodal imaging when aggregation is imminent, enabling intelligent Brillouin microscopy of this dynamic biomechanical process. Furthermore, we demonstrate that by detecting mature aggregates in real time using brightfield images and a neural network, Brillouin microscopy can be used to study their biomechanical properties without the need for fluorescence labeling, minimizing phototoxicity and preserving sample health. This autonomous microscopy approach advances the study of aggregation kinetics and biomechanics in living cells, offering a powerful tool for investigating the role of protein misfolding and aggregation in neurodegeneration.

Suggested Citation

  • Khalid A. Ibrahim & Camille Cathala & Carlo Bevilacqua & Lely Feletti & Robert Prevedel & Hilal A. Lashuel & Aleksandra Radenovic, 2025. "Self-driving microscopy detects the onset of protein aggregation and enables intelligent Brillouin imaging," Nature Communications, Nature, vol. 16(1), pages 1-10, December.
  • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-60912-0
    DOI: 10.1038/s41467-025-60912-0
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    References listed on IDEAS

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    1. Nathan Riguet & Anne-Laure Mahul-Mellier & Niran Maharjan & Johannes Burtscher & Marie Croisier & Graham Knott & Janna Hastings & Alice Patin & Veronika Reiterer & Hesso Farhan & Sergey Nasarov & Hila, 2021. "Nuclear and cytoplasmic huntingtin inclusions exhibit distinct biochemical composition, interactome and ultrastructural properties," Nature Communications, Nature, vol. 12(1), pages 1-27, December.
    2. Audrey Durand & Theresa Wiesner & Marc-André Gardner & Louis-Émile Robitaille & Anthony Bilodeau & Christian Gagné & Paul De Koninck & Flavie Lavoie-Cardinal, 2018. "A machine learning approach for online automated optimization of super-resolution optical microscopy," Nature Communications, Nature, vol. 9(1), pages 1-16, December.
    3. Jes Dreier & Marco Castello & Giovanna Coceano & Rodrigo Cáceres & Julie Plastino & Giuseppe Vicidomini & Ilaria Testa, 2019. "Smart scanning for low-illumination and fast RESOLFT nanoscopy in vivo," Nature Communications, Nature, vol. 10(1), pages 1-11, December.
    4. Montserrat Arrasate & Siddhartha Mitra & Erik S. Schweitzer & Mark R. Segal & Steven Finkbeiner, 2004. "Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death," Nature, Nature, vol. 431(7010), pages 805-810, October.
    5. Khalid A. Ibrahim & Kristin S. Grußmayer & Nathan Riguet & Lely Feletti & Hilal A. Lashuel & Aleksandra Radenovic, 2023. "Label-free identification of protein aggregates using deep learning," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
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