Amyloid fibrils are insoluble protein aggregates comprised of highly ordered β-sheet structures and they are involved in the pathology of amyloidoses, such as Alzheimer's disease. A supramolecular strategy is presented for inhibiting amyloid fibrillation by using cucurbituril (CB). CB prevents the fibrillation of insulin and β-amyloid by capturing phenylalanine (Phe) residues, which are crucial to the hydrophobic interactions formed during amyloid fibrillation. These results suggest that the Phe-specific binding of CB can modulate the intermolecular interaction of amyloid proteins and prevent the transition from monomeric to multimeric states. CB thus has potential for the development of a therapeutic strategy for amyloidosis.
- supramolecular chemistry
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