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Supramolecular Inhibition of Amyloid Fibrillation by Cucurbit[7]uril

Title
Supramolecular Inhibition of Amyloid Fibrillation by Cucurbit[7]uril
Authors
Lee, HHChoi, TSLee, SJCLee, JWPark, JKo, YHKim, WJKim, KKim, HI
POSTECH Authors
Kim, WJKim, KKim, HI
Date Issued
Jul-2014
Publisher
WILEY-V C H VERLAG GMBH
Abstract
Amyloid fibrils are insoluble protein aggregates comprised of highly ordered beta-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 beta-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.
Keywords
aggregation; beta-amyloid; cucurbit[7]uril; insulin; supramolecular chemistry; INSULIN; COMPLEXES; CHEMISTRY; PROTEINS
URI
http://oasis.postech.ac.kr/handle/2014.oak/13768
DOI
10.1002/ANIE.201402496
ISSN
1433-7851
Article Type
Article
Citation
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, vol. 53, no. 29, page. 7461 - 7465, 2014-07
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김기문KIM, KIMOON
Dept of Chemistry
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