Abstract
Defining pathways for amyloid assembly could impact therapeutic strategies for as many as 50 disease states. Here we show that amyloid assembly is subject to different forces regulating nucleation and propagation steps and provide evidence that the more global β-sheet/β-sheet facial complementarity is a critical determinant for amyloid nucleation and structural selection.
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 / chemical synthesis*
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Amyloid / chemistry*
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Amyloid beta-Peptides / chemistry
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Amyloid beta-Peptides / metabolism
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Amyloidogenic Proteins / chemistry*
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Amyloidogenic Proteins / metabolism
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Humans
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Protein Structure, Secondary
Substances
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Amyloid
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Amyloid beta-Peptides
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Amyloidogenic Proteins