A groundbreaking new study being called a "world-first achievement" provided humanity with a glimpse into the molecular chemistry of the human brain — and its findings could help scientists tackle Alzheimer's disease.
The study, originally published in the journal Nature , takes a look at the cells that make up the brain, scrutinizing the proteins involved in their functioning . Researchers at the University of Leeds and some collaborators used a new cutting-edge technology that allowed them to observe even the tiniest of brain structures.
"Here, using cryo-fluorescence microscopy-targeted cryo-sectioning, cryo-focused ion beam-scanning electron microscopy lift-out and cryo-electron tomography, we determined in-tissue architectures of β-amyloid and tau pathology in a postmortem Alzheimer’s disease donor brain," the authors of the study wrote in its abstract. Such technology, in simpler terms, involves using a microscope that can work at extremely cold temperatures, which are necessary to preserve the structure of dead human brains.
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They explained, "A defining pathological feature of most neurodegenerative diseases is the assembly of proteins into amyloid that form disease-specific structures. In Alzheimer’s disease, this is characterized by the deposition of β-amyloid and tau with disease-specific conformations. The in situ structure of amyloid in the human brain is unknown."
Buildups of both β-amyloid plaques and tau clusters in the brain are thought to damage brain cells and clog up neural pathways, leading to the symptoms of Alzheimer's like memory loss and confusion by killing cells beyond the blockages. Such buildups can also lead to symptoms of other neurodegenerative diseases.
The study sought to analyze their structure so that researchers could better develop medicines that could clear out blockages caused by too much of a given protein, which could then potentially alleviate the effects of Alzheimer's, or, at the very least, slow it down.
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Researchers found that the β-amyloid plaques had fibrils, many of which were "branched," and that they also contained protofilaments that were "arranged in parallel arrays and lattice-like structures." Tau clusters instead had "unbranched" filaments, with polypeptide backbones, with similarities between filaments in clusters but not between the clusters themselves.
The 3D maps the study allowed the UK team to develop could be crucial in developing medications that can help treat Alzheimer's and a wider array of diseases. "The in situ structural approaches outlined here for human donor tissues have applications to a broad range of neurodegenerative diseases," the authors of the study wrote.
Dr. Rene Frank, the study's lead author and an associate professor at the University of Leeds' School of Biology, summed up the study's findings in a media release, "This first glimpse of the structure of molecules inside the human brain offers further clues to what happens to proteins in Alzheimer's disease but also sets out an experimental approach that can be applied to better understand a broad range of other devastating neurological diseases."
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