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}) })(jQuery); </script> </head> <body class="post-template-default single single-post postid-187 single-format-standard header-image full-width-content genesis-breadcrumbs-visible"><div class="site-container"><header class="site-header"><div class="wrap"><div class="title-area"><p class="site-title"><a href="https://www.thermofisher.com/" title="Thermo Fisher Scientific">Thermo Fisher Scientific</a></p><p class="site-description">Electron and cryo-electron microscopy stories and solutions about the advancement of cellular and structural biology</p></div><div class="widget-area header-widget-area"><section id="block-5" class="widget widget_block"><div class="widget-wrap"> <div class="wp-block-group"><div class="wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow"></div></div> </div></section> <section id="block-6" class="widget widget_block"><div class="widget-wrap"> <div class="wp-block-group"><div class="wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow"></div></div> </div></section> </div><div class="breadcrumb"><span class="breadcrumb-link-wrap"><a href="https://www.thermofisher.com/blog/?">Accelerating Science</a></span><span class="breadcrumb-link-wrap"><a class="breadcrumb-link" href="https://www.thermofisher.com/blog/atomic-resolution/"><span class="breadcrumb-link-text-wrap">Life in Atomic Resolution</span></a><meta ></span> <span aria-label="breadcrumb separator">/</span> <span class="breadcrumb-link-wrap"><a class="breadcrumb-link" href="https://www.thermofisher.com/blog/atomic-resolution/cryo-electron-microscopy-cryo-em/"><span class="breadcrumb-link-text-wrap">Cryo-Electron Microscopy (Cryo-EM)</span></a><meta ></span> <span aria-label="breadcrumb separator">/</span> <span class="breadcrumb-current-title">Cryo-EM Helps Researchers Understand the Underlying Science Behind Alzheimer鈥檚</span></div></div></header><div class="site-inner"><div class="content-sidebar-wrap"><main class="content"><article class="post-187 post type-post status-publish format-standard has-post-thumbnail category-cryo-electron-microscopy-cryo-em category-unlocking-the-mysteries-with-cryo-em tag-alzheimers tag-brain-prize tag-cryo-electron-microscopy tag-cryo-em tag-electron-microscopy tag-fei tag-ide tag-mrc-laboratory-of-molecular-biology tag-tau-proteins tag-thermo-fisher-scientific tag-thermo-scientific tag-unlocking-the-mysteries entry" aria-label="Cryo-EM Helps Researchers Understand the Underlying Science Behind Alzheimer鈥檚"><header class="entry-header"><h1 class="entry-title">Cryo-EM Helps Researchers Understand the Underlying Science Behind Alzheimer鈥檚</h1> <span class="post-info-author"> By <a href="https://www.thermofisher.com/blog/author/gabriellakiss/" title="Posts by Gabriella Kiss" rel="author">Gabriella Kiss</a> </span> <span class="post-info-date"> 01.14.2019 </span> </header><div class="entry-content"><p>A progressive brain disease that slowly erodes thinking skills and the ability to perform simple tasks, Alzheimer鈥檚 disease can cause great distress to both victims and their family members. Today, 50 million people worldwide have dementia, about two-thirds of whom suffer from Alzheimer鈥檚, according to the <a href="https://www.alz.co.uk/research/WorldAlzheimerReport2018.pdf">World Alzheimer Report 2018</a>. And unfortunately, the number of cases is expected to triple to 152 million by 2050.</p> <p>Alzheimer鈥檚 disease was first identified in 1906. Yet, over 100 years later, we still don鈥檛 know what causes this neurodegenerative disease. As with any serious illness, however, the more clearly scientists understand how Alzheimer鈥檚 is structured and how it functions, the closer they will be to discovering the underlying cause, developing effective treatments, and learning how to prevent or cure the disease.</p> <p><a href="https://ter.li/mjl5gm">Cryo-electron microscopy</a> (cryo-EM) is opening new pathways for scientists working to advance Alzheimer鈥檚 research and develop a more detailed understanding of what causes the disease and how it damages human brain cells. One <a href="https://ter.li/pxtyjj">recent study</a>聽explores how insulin degrading enzyme (IDE) plays a key role in degrading peptides that are critical in Alzheimer’s and several other human diseases.</p> <div style="width: 640px;" class="wp-video"> <video class="wp-video-shortcode" id="video-187-1" width="640" height="484" preload="metadata" controls="controls"><source type="video/mp4" src="https://www.thermofisher.com/blog/wp-content/uploads/sites/12/2019/01/alzheimers-video.mp4?_=1" /><a href="https://www.thermofisher.com/blog/wp-content/uploads/sites/12/2019/01/alzheimers-video.mp4">https://www.thermofisher.com/blog/wp-content/uploads/sites/12/2019/01/alzheimers-video.mp4</a></video></div> <p style="text-align: center"><em>Overall fit of human dimeric IDE structures with the electron density maps via DOI 10.7554/eLife.33572.016</em></p> <p>Another area of Alzheimer鈥檚 research is exploring how tau proteins within brain cells cease their usual protective function and aggregate to form large tangles that disrupt the shape and function of the cells, eventually killing them. Researchers believe these damaged cells cause the kind of destructive degeneration seen in the brains of dementia patients.</p> <p>Using cryo-EM, researchers from the Medical Research Council’s Laboratory of Molecular Biology (LMB) in Cambridge, UK <a href="https://ter.li/7jdpsp">solved the structure of dementia-causing tau proteins</a> in unprecedented detail鈥攁 breakthrough that was partly responsible for Professor Michel Goedert becoming a <a href="https://ter.li/wvhirq">co-recipient of the 2018 Brain Prize</a>. Working with brain tissue from a deceased 74-year-old Alzheimer鈥檚 patient, the team used cryo-EM to isolate tau proteins and explore their structure.</p> <p><img decoding="async" class="aligncenter" style="margin-left: auto;margin-right: auto" src="https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2022/04/structure-of-tau-filaments-from-alzheimers-brain-solved-by-cryo-em-290157.png" /></p> <p style="text-align: center"><em>Using cryo-EM, researchers solved the structure of tau filament structures, rendered in blue and white in this photo. Knowing how tau proteins assemble into their filaments is expected to lead to more targeted treatment of Alzheimer鈥檚.</em><em>(Source: <a href="https://ter.li/u4k5s2">Technology Networks</a>)</em></p> <p>Previous efforts to solve the structure of tau proteins were limited by technology and required proteins in much larger amounts than those produced in a diseased brain. As a result, researchers had to create proteins in a laboratory and force the filaments to aggregate in a dish. Although this work led to valuable insights, the question of whether the tau filaments aggregate the same way in a human brain remained unanswered. With cryo-EM, the LMB researchers needed far less protein, so they could take their samples directly from a diseased human brain and use them to solve the structure of tau proteins at near-atomic level.</p> <p>For several decades, researchers have known that the abnormal assembly of tau protein into filaments is a defining characteristic of Alzheimer鈥檚. Understanding the structure of these filaments is seen as crucial in developing drugs that can prevent their formation.</p> <p>Cryo-EM offers a clearer picture of the underlying science behind Alzheimer鈥檚. By understanding the structure of proteins in unprecedented detail, researchers can more closely pinpoint how alterations in their structures affect their function鈥攗nlocking the mysteries behind Alzheimer鈥檚 and other diseases at a much faster rate than was previously possible.</p> <p><a href="https://www.thermofisher.com/blog/microscopy/using-cryo-em-to-uncover-changes-in-the-brain-in-parkinsons-victims/?cid=blog-alzheimers-ctaimage"><img decoding="async" class="aligncenter size-full wp-image-556" src="https://www.thermofisher.com/blog/atomic-resolution/wp-content/uploads/sites/22/2022/04/parkinsons-1.jpg" alt="parkinsons" width="703" height="372" /></a></p> <p><em>Looking to learn more about our </em><em><a href="https://ter.li/p35139">Unlocking the Mysteries blog series</a></em><em>? Stay tuned for the next post in our blog series, where we鈥檙e showing how electron microscopy is advancing science and solving some of the world鈥檚 most complex challenges. </em><a href="https://eur03.safelinks.protection.outlook.com/?url=https%3A%2F%2Fwww.thermofisher.com%2Fblog%2Fmicroscopy%2F%3Fcid%3Dblog-conclusion&data=02%7C01%7C%7C29aacc2aba0247dfe47508d66057dc4d%7C84df9e7fe9f640afb435aaaaaaaaaaaa%7C1%7C0%7C636802327799069889&sdata=WqypQznM8gBsqeX7XzAaTbfTamBT2JrAifT%2Bf1yzHGs%3D&reserved=0"><em>Subscribe now</em></a><em> to receive new Accelerating Microscopy posts straight to your inbox. </em></p> <p><em>Gabriella Kiss, PhD, is a Product Marketing Manager for Single Particle Workflow at Thermo Fisher Scientific.</em></p> <p>To learn more about cryo-EM, <a href="https://ter.li/zfr3wq">fill out this form</a> to speak with an expert.</p>  <div class="jp-relatedposts"> <div class="related-post related-1"> <a 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