Abstract
We describe coumarin derivatives that are non-fluorescent in aqueous buffers and that very selectively bind to transthyretin (TTR) in complex biological environments potently inhibiting TTR amyloidogenesis while also exhibiting sensitive off-on fluorescent sensing of the properly folded quaternary structure of TTR.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amyloid / antagonists & inhibitors
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Amyloid / metabolism*
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Coumarins / chemistry*
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Escherichia coli / metabolism
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Humans
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Prealbumin / antagonists & inhibitors*
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Prealbumin / metabolism
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Protein Binding
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Protein Folding
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Protein Structure, Quaternary
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Spectrometry, Fluorescence
Substances
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Amyloid
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Coumarins
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Prealbumin
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coumarin