Dear colleagues,

 

Department of Chemistry cordially invite you to the Physical Chemistry seminar that will be given by Dr. Ujjayini Ghosh on Thursday, Feb 27 at 4:10 pm, CEM 136.

 

Dr. Ujjayini Ghosh is currently a postdoctoral fellow with Professor David Weliky in the Department of Chemistry at MSU. After obtaining her PhD in physical chemistry from MSU, she worked with Dr. Robert Tycko 'in the Chemical Physics Laboratory at NIDDK NIH as a postdoctoral fellow. Her talk on Thursday will feature a cutting-edge study combining cryo-EM and solid-state NMR to elucidate the high-resolution structure of amyloid-beta fibrils directly obtained from post-mortem brain of patients with Alzheimer's diseases. We hope that many good scientific discussions and feedback can be made. 

 

Thank you very much!

 

Best regards,

Heedeok

 

 

 

 

 

 

Seminar

Integrated Cryo-EM and Solid-State NMR Structure of Amyloid-β Fibrils from Alzheimer’s Disease Brain

 

Dr. Ujjayini Ghosh^1,2

¹Laboratory of Chemical Physics, NIDDK, National Institutes of Health

²Department of Chemistry, Michigan State University

 

Amyloid fibril formation by various polypeptides is a biophysically interesting and biomedically important phenomenon, any understanding of which depends on molecular structural information. The aggregation of amyloid-β (Aβ) peptide in the brain as amyloid fibrils is a pathological hallmark of Alzheimer’s disease. Structural studies of these aggregates are important in understanding their formation, spreading, and for development of therapeutic and diagnostic approaches. In this talk, I will describe the structural studies of Aβ-fibrils from the postmortem brain of an individual with Alzheimer’s disease. Here we have integrated both solid-state NMR (ssNMR) and cryoEM to solve the structure of the most common polymorph of Aβ-fibrils that develop in the brain of Alzheimer’s disease patients. Here we present the cryoEM map of Aβ-fibril at 2.7 Å resolution. The information from both ssNMR and cryoEM are combined in a single structure calculation to obtain the structure of brain-derived Aβ-fibrils. In the case of Aβ fibrils, we have found a surprising two-fold symmetric polymorph with a mass-per-length value of 27 kDa/nm (indicating three Aβ molecules per β-sheet repeat spacing). The integration of cryoEM and ssNMR pave the way for structural studies of complex systems.

 

THURSDAY, FEBRUARY 27, 2020

4:10 PM

Room 136 – Chemistry

David Weliky – Host