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Supramolecular Inhibition of Amyloid Fibrillation by Cucurbit[7]uril
Author(s) -
Lee Hong Hee,
Choi Tae Su,
Lee Shin Jung C.,
Lee Jong Wha,
Park Junghong,
Ko Young Ho,
Kim Won Jong,
Kim Kimoon,
Kim Hugh I.
Publication year - 2014
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201402496
Subject(s) - amyloid (mycology) , fibrillation , chemistry , fibril , amyloid fibril , supramolecular chemistry , monomer , amyloidosis , biophysics , biochemistry , amyloid β , crystallography , disease , biology , organic chemistry , medicine , crystal structure , atrial fibrillation , inorganic chemistry , polymer
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 cucurbit[7]uril (CB[7]). CB[7] 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[7] can modulate the intermolecular interaction of amyloid proteins and prevent the transition from monomeric to multimeric states. CB[7] thus has potential for the development of a therapeutic strategy for amyloidosis.