Protein Misfolding and Alzheimer's, Huntington's, Mad Cow and Cataracts       


Medical, Health Informatics and Computational Biology Accomplishment | 2011

IBM researchers: Ruhong Zhou, Payel Das, Bruce Berne, Ajay Royyuru, Tien Huynh

Where the work was done: IBM T.J. Watson Research Center

What we accomplishedMany fatal diseases are closely related to protein misfolding and aggregation, such as Alzheimer’s, Huntington’s, Mad Cow and cataracts. Understanding the molecular mechanism by which those pathological proteins aggregate is a necessary step for preventing and/or treating these diseases. In collaboration with experimental labs at MIT, Columbia, Harvard, and UCSB, IBM has conducted theoretical studies using large-scale atomic-level simulations to investigate the relationship between folding and misfolding of these proteins.

These unprecedented molecular dynamics simulations unravel the mechanism of Abeta-peptides aggregation in Alzheimer’s and lens gamma-crystallin polymerization in cataracts for the first time. These findings provide physical insights into the pathogenesis of not only Alzheimer’s and cataract but also of other diseases involving protein clumping such as Huntington’s and Mad Cow diseases.

Related link: PNAS 2011: “Aggregation of Partially Folded gamma-Crystallin Associated with Human Cataracts via Domain Swapping at the C-terminal beta-strands” (50 citations, 2/15/2016)

Image credit: TechGlimpse

 

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