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Study reveals how the world's first drug for amyloid disease works
Date:5/29/2012

ed interesting biochemical stabilization, Wilson's team analyzed its structure. "By the end, we had determined more than 30 small molecule stabilizerTTR structures, in an effort to generate tafamidis and identify the molecular interactions that lead to stabilization of the natural TTR tetramer," said Stephen Connelly, a Wilson laboratory staff scientist who performed these structural studies and who was a co-author the paper.

The small molecule benzoxazole, tafamidis, that ultimately entered clinical trials was optimized for several criteria, including its ability to stabilize the TTR tetramer's weakest seam. "We found that one end of the tafamidis structure fits neatly into the tetramer's hydrophobic thyroxine-binding pocket, while at the other end it binds to nearby polar amino acids, both types of interactions bridging or stabilizing the two halves of the tetramer," Connelly said. The drug's stabilizing force greatly reduces the rate at which these tetramers come apart, and in so doing greatly reduces the rate of amyloid formation.

Tafamidis is considered an "orphan" drug because its initial intended treatment population is the relatively small polyneuropathy population. However, even wild-type TTR forms amyloid in 10 to 20 percent of the growing elderly populationleading to cardiomyopathy. Thus, this condition, and drugs such as tafamidis that can treat it, could be of growing interest to the pharmaceutical industry.


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Contact: Mika Ono
mikaono@scripps.edu
858-784-2052
Scripps Research Institute
Source:Eurekalert  

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