Mutual chaperoning by amyloid forming proteins/peptides

author: Eva Žerovnik, Department of Biochemistry and Molecular Biology, Jožef Stefan Institute
published: Oct. 1, 2015,   recorded: May 2015,   views: 1198


Related Open Educational Resources

Related content

Report a problem or upload files

If you have found a problem with this lecture or would like to send us extra material, articles, exercises, etc., please use our ticket system to describe your request and upload the data.
Enter your e-mail into the 'Cc' field, and we will keep you updated with your request's status.
Lecture popularity: You need to login to cast your vote.


We study the mechanisms of protein aggregation and cellular toxicity by the prefibrillar oligomers formed intracellularly by amyloidogenic proteins and some of their pathological mutants. It is an accepted view that the most toxic are soluble oligomers in range of 6 to 30 mers, that are membrane seeking and even make pores into membranes (1-2). I will discuss the proposal that changed pre-amyloidogenic conformations of amyloid forming proteins may act as mutual chaperones, leading to temporary inhibition of aggregation and toxicity. Examples will be described of crystallins, prion protein and stefin B; all binders of amyloid-beta (3). Small molecule inhibitors of protein aggregation will also be discussed. Our main model protein from the family of cystatins, stefin B will be described in more detail. It’s possible function in the cell’s response to protein mis-folding will be high-lighted (4).

Link this page

Would you like to put a link to this lecture on your homepage?
Go ahead! Copy the HTML snippet !

Write your own review or comment:

make sure you have javascript enabled or clear this field: