Suppression of amyloid-β fibril growth by drug-engineered polymorph transformation

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SUMMARY

    The authors demonstrate that bexarotene, a T-cell lymphoma medication with known antiamyloid activity both in_vitro and in_vivo, suppresses amyloid fibrillization by promoting an alternative fibril structure. The authors find that the suppression of fibril growth by bexarotene is not because of the drug binding to the fibril tips or to the peptides in the solution. As an additional benefit, the bexarotene fibrils kill primary rat hippocampal neurons less efficiently than normal fibrils. Finding the lowest concentration for net fibril growth defines the fibril solubility and quantifies the equilibrium_constant for fibril growth and the . . .

     

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