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Towards a pharmacophore for amyloid.

<div class='caption-title'>The crystal structure of the KLVFFA segment from Aβ complexed with orange-G.</div>
<div class='caption-title'>Binding cavities of orange-G within fibers of the KLVFFA segment from Aβ.</div>
<div class='caption-title'>Small molecule binding is specific for fiber polymorphism.</div>
Landau M, Sawaya MR, Faull KF, Laganowsky A, Jiang L, Sievers SA, Liu J, Barrio JR, Eisenberg D
OpenAccess logo PLoS Biol 9 e1001080 (2011)
Cited: 98 times
EuropePMC logo PMID: 21695112

Abstract

Diagnosing and treating Alzheimer's and other diseases associated with amyloid fibers remains a great challenge despite intensive research. To aid in this effort, we present atomic structures of fiber-forming segments of proteins involved in Alzheimer's disease in complex with small molecule binders, determined by X-ray microcrystallography. The fiber-like complexes consist of pairs of β-sheets, with small molecules binding between the sheets, roughly parallel to the fiber axis. The structures suggest that apolar molecules drift along the fiber, consistent with the observation of nonspecific binding to a variety of amyloid proteins. In contrast, negatively charged orange-G binds specifically to lysine side chains of adjacent sheets. These structures provide molecular frameworks for the design of diagnostics and drugs for protein aggregation diseases.

Reviews - 3ovl mentioned but not cited (2)

  1. NMR Meets Tau: Insights into Its Function and Pathology. Lippens G, Landrieu I, Smet C, Huvent I, Huvent I, Gandhi NS, Gigant B, Despres C, Qi H, Lopez J. Biomolecules 6 (2016)
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Articles - 3ovl mentioned but not cited (9)

  1. Towards a pharmacophore for amyloid. Landau M, Sawaya MR, Faull KF, Laganowsky A, Jiang L, Sievers SA, Liu J, Barrio JR, Eisenberg D. PLoS Biol. 9 e1001080 (2011)
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Reviews citing this publication (25)

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