Abstract
Using NMR to probe transient binding of Aβ1-40 monomers to fibers, we find partially bound conformations with the highest degree of interaction near F19-K28 and a lesser degree of interaction near the C-terminus (L34-G37). This represents a shift away from the KLVFFA recognition sequence (residues 16-21) currently used for inhibitor design.
MeSH terms
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Amino Acid Sequence
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Amyloid beta-Peptides / chemistry*
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Amyloid beta-Peptides / metabolism
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Microscopy, Electron
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Nuclear Magnetic Resonance, Biomolecular*
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Peptide Fragments / chemistry*
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Peptide Fragments / metabolism
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Protein Aggregates
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Sonication
Substances
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Amyloid beta-Peptides
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Peptide Fragments
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Protein Aggregates
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amyloid beta-protein (1-40)