Innovation Anthology #278:
When normal prion proteins misfold, they may become infectious and lead to deadly diseases like Mad Cow, Chronic wasting and Variant Creuztfeld-Jacob Disease.
Working at the atomic scale, Dr. David Wishart from the University of Alberta has identified that the tail end of the prion molecule may be the part that disrupted first.
DR. DAVID WISHART: It aggregates first in what we call dymers or pairs, then in techamers or sets of four, and then ultimately in octomers, or groups of eight molecules. And that these aggregates are all hung together near the back end from last to about 70 residues. So they produce this insoluable, tightly massed core, that can’t be cut, that can’t be broken down. Then these octomers eventually start forming fibrils or threads. And this process is very mysterious and seems to take weeks, months perhaps.
Dr. David Wishart says this discovery may help researchers develop vaccines or small molecule drugs to stop the misfolding process.
Thanks today to the Canadian Institutes of Health Research.
FOR INNOVATION ANTHOLOGY
I’M CHERYL CROUCHER
Guest
,
, , , ,
Sponsor
Canadian Institutes of Health Research
Program Date: 2009-12-22