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

uded in the TTR aggregate distribution are amyloid fibrilsprotein stacks made from millions of TTR monomersalthough researchers suspect that smaller, shorter-lived pre-amyloid aggregates do more direct damage to nerve cells and nerve fibers.

The early onset TTR amyloidoses are caused by inherited TTR mutations that weaken the tetramers' ability to stick together, producing monomers more likely to aggregate into amyloids and other aggregate structures. Fortunately, the TTR tetramer, which is the backup carrier of the thyroid hormone thyroxine through the bloodstream, has two unoccupied thyroxine-binding sites along its longest and weakest seam. Kelly and his colleagues designed tafamidis to grab either of these thyroxine-binding sites, in a way that bridges the seam and helps keep the tetramer from coming apart.

A Stabilizing Influence

The newly published molecular and structural data show that tafamidis does indeed stabilize TTR tetramers, under normal physiological conditions in the bloodstream and even under abnormal conditions when they would be much more likely to fall apart and reassemble as amyloids. Tafamidis has this stabilizing effect on tetramers of the normal "wild-type" TTR protein as well as on those made from disease-associated mutant and wild type TTR subunits.

"There are more than a hundred TTR mutations that cause amyloidosis, but the vast majority of those TTRs are capable of being bound by tafamidis and held in the natural tetramer state," said Kelly.

Throughout the development of tafamidis-type compounds, Kelly and his colleagues collaborated with the Scripps Research laboratory of Ian A. Wilson, who is Hansen Professor of Structural Biology and a member of the Skaggs Institute at Scripps Research. The Wilson laboratory specializes in the use of X-ray crystallography to determine the atomic structures of interacting proteins. Whenever a small molecule stabilizer of TTR was generated that afford
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Contact: Mika Ono
mikaono@scripps.edu
858-784-2052
Scripps Research Institute
Source:Eurekalert  

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