{"id":49779,"date":"2020-06-29T00:00:00","date_gmt":"2020-06-28T23:00:00","guid":{"rendered":"http:\/\/www.pcb.ub.edu\/a-new-mechanism-of-toxicity-in-alzheimers-disease-has-been-%e2%80%a8revealed\/"},"modified":"2020-11-18T15:03:00","modified_gmt":"2020-11-18T14:03:00","slug":"a-new-mechanism-of-toxicity-in-alzheimers-disease-has-been-%e2%80%a8revealed","status":"publish","type":"post","link":"https:\/\/www.pcb.ub.edu\/en\/a-new-mechanism-of-toxicity-in-alzheimers-disease-has-been-%e2%80%a8revealed\/","title":{"rendered":"A new mechanism of toxicity in Alzheimer’s disease has been \u2028revealed"},"content":{"rendered":"

The brains of millions of people suffering from Alzheimer\u00b4s disease (AD) are slowly and inescapably being depleted of neurons, which leads to the characteristic loss of memory and cognitive function associated with this condition. However, the cause of neuronal death is still unknown. The treatments available are aimed at slowing down the development of dementia and only help to improve quality of life for short periods. Therefore, treatments to actually cure AD are an unmet medical need.<\/p>\n

Researchers led by\u00a0Natalia Carulla, IRB Barcelona Alumni, former group leader at the Institut Europ\u00e9en de Chimie et Biologie (IECB) in Bordeaux, and currently project manager at Grup CIEF have revealed for the first time the atomic structure of amyloid-beta (A\u03b2) protein assemblies.<\/p>\n

The knowledge of this structure reveals a new mechanism of toxicity for these assemblies, with the capacity to disrupt the neuronal membrane, allowing water and ions to pass through it and causing the death of these cells. Several studies have proposed that the interaction of the A\u03b2 protein with the neuronal membrane is responsible for the neuronal death observed in AD. However, the A\u03b2 protein is a difficult therapeutic target because it is \u201csticky\u201d and self-assembles, adopting distinct shapes and sizes.<\/p>\n

\u201cKnowing the features that characterise these protein ensembles, such as the number of molecules that make them and the shape they adopt, is crucial to design effective therapeutic strategies that target the forms of A\u03b2 ensembles responsible for the neurotoxicity in AD,\u201d\u00a0Carulla\u00a0explains.<\/p>\n

\nAn in vitro approach to ensure stable A\u03b2 forms<\/strong><\/span><\/p>\n

To tackle the instability of the different conformations, the team first studied the A\u03b2 protein in vitro\u2014in simplified model systems that mimic the neuronal membrane\u2014to develop conditions to prepare stable A\u03b2 forms of uniform composition and shape. Once the different compositions had been identified, they studied their structure and mode of neurotoxicity, establishing a 3D arrangement of all the atoms making up the A\u03b2 ensemble.<\/p>\n

\u201cOur study suggests that some A\u03b2 associations can perforate the membrane of neurons, alter their osmotic equilibrium, and consequently trigger their death,\u201d say\u00a0Sonia Ciudad\u00a0and\u00a0Eduard Puig, first authors of the paper.\u00a0Ciudad\u00a0is an IRB Barcelona Alumni, currently R&D Scientist at Biokit, a Werfen Company; while\u00a0Puig\u00a0is now a postdoctoral fellow in Research Unit on Asymmetric Synthesis at IRB Barcelona.<\/p>\n

\n\u25ba Reference article: <\/strong>Sonia Ciudad, Eduard Puig, Thomas Botzanowski, Moeen Meigooni, Andres S. Arango, Jimmy Do, Maxim Mayzel, Mariam Bayoumi, St\u00e9phane Chaignepain, Giovanni Maglia, Sarah Cianferani, Vladislav Orekhov, Emad Tajkhorshid, Benjamin Bardiaux & Nat\u00e0lia Carulla. “A\u03b2(1-42) tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage<\/a>“. Nature Communications (2020) DOI:10.1038\/s41467-020-16566-1<\/p>\n

\u25ba More information: IRB Barcelona website [+]<\/a><\/strong><\/p>\n

\u00a0<\/p>\n","protected":false},"excerpt":{"rendered":"

An international team of researchers led by Natalia Carulla, IRB Barcelona Alumni<\/a>,<\/a> reveals that specific amyloid-beta (A\u03b2) protein ensembles have the capacity to disrupt the membrane of neurons, causing their death.This finding, published in the journal Nature communications, could make a significant breakthrough in the treatment of Alzheimer\u00b4s disease.<\/p>\n

\u00a0<\/p>\n","protected":false},"author":1,"featured_media":54194,"comment_status":"closed","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"inline_featured_image":false,"footnotes":""},"categories":[8],"tags":[],"class_list":["post-49779","post","type-post","status-publish","format-standard","has-post-thumbnail","category-uncategorized"],"acf":[],"yoast_head":"\nA new mechanism of toxicity in Alzheimer's disease has been \u2028revealed - Parc Cient\u00edfic de Barcelona<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/www.pcb.ub.edu\/en\/a-new-mechanism-of-toxicity-in-alzheimers-disease-has-been-\u2028revealed\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"A new mechanism of toxicity in Alzheimer's disease has been \u2028revealed - 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