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Supramolecular Inhibition of Amyloid Fibrillation by Cucurbit[7]uril

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Title
Supramolecular Inhibition of Amyloid Fibrillation by Cucurbit[7]uril
Author(s)
Hong Hee Lee; Tae Su Choi; Shin Jung C. Lee; Jong Wha Lee; Junghong Park; Yong Ho Ko; Won Jong Kim; Kimoon Kim; Hugh I. Kim
Subject
aggregation · b-amyloid · cucurbit[7]uril · insulin ·supramolecular chemistry
Publication Date
2014-07
Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, v.53, no.29, pp.7461
Publisher
WILEY-V C H VERLAG GMBH
Abstract
Amyloid fibrils are insoluble protein aggregates comprised of highly ordered b-sheet structures and they are involved in the pathology of amyloidoses, such as Alzheimers 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 b-amyloid by capturing phenylalanine (Phe) residues, which are crucial to the hydro- phobic 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.
URI
https://pr.ibs.re.kr/handle/8788114/987
DOI
10.1002/anie.201402496
ISSN
1433-7851
Appears in Collections:
Center for Self-assembly and Complexity(복잡계 자기조립 연구단) > 1. Journal Papers (저널논문)
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