Supramolecular Inhibition of Amyloid Fibrillation by Cucurbit[7]uril
SCIE
SCOPUS
- Title
- Supramolecular Inhibition of Amyloid Fibrillation by Cucurbit[7]uril
- Authors
- Lee, HH; Choi, TS; Lee, SJC; Lee, JW; Park, J; Ko, YH; Kim, WJ; Kim, K; Kim, HI
- Date Issued
- 2014-07-14
- 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
- https://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, 2014-07-14
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- There are no files associated with this item.
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