{"id":214,"date":"2013-09-30T11:02:23","date_gmt":"2013-09-30T11:02:23","guid":{"rendered":"http:\/\/blogs.kent.ac.uk\/biosciences\/?p=214"},"modified":"2013-10-07T11:14:51","modified_gmt":"2013-10-07T11:14:51","slug":"research-seminar-protein-and-metal-ion-interactions-with-the-alzheimers-amyloid-beta-peptide-ab","status":"publish","type":"post","link":"https:\/\/blogs.kent.ac.uk\/biosciences\/2013\/09\/30\/research-seminar-protein-and-metal-ion-interactions-with-the-alzheimers-amyloid-beta-peptide-ab\/","title":{"rendered":"Research Seminar: Protein and metal ion interactions with the Alzheimer’s Amyloid-beta Peptide"},"content":{"rendered":"

Dr. John Viles, School of Biological and Chemical Sciences, Queen Mary, University of London<\/strong><\/p>\n

The key hallmark of Alzheimer\u2019s disease is the formation of amyloid-beta peptide\u00a0fibers and oligomers.\u00a0 This process is often considered in isolation but there is now clear evidence that in vivo\u00a0amyloid-beta peptide will bind to other proteins and metal ions.\u00a0 I will focuses on two clearly identified protein partners for amyloid-beta peptide. Human serum albumin; the most abundant protein in cerebral spinal fluid (CSF) within the brain and the prion protein (PrP), concentrated at the synaptic terminals with a high affinity for amyloid-beta peptide.\u00a0 The lecture will focus on biophysical approaches to understanding these fundamental interactions.<\/p>\n

Monday 14th October 2013, 4.00 p.m. in Ingram Lecture Theatre<\/p>\n

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