한빛사논문
- 조회1,333
Abstract
Hong Hee Lee1,‡, Tae Su Choi1,‡, Shin Jung C. Lee1, Jong Wha Lee1, Junghong Park1,2, Dr. Young Ho Ko2, Prof. Dr. Won Jong Kim1,2, Prof. Dr. Kimoon Kim1,2,3,* and Prof. Dr. Hugh I. Kim1,3,*
1 Department of Chemistry, Pohang University of Science and Technology, Pohang, 790-784 (Republic of Korea)
2 Center for Self-assembly and Complexity, Institute for Basic Science, Pohang University of Science and Technology, Pohang, 790-784 (Republic of Korea)
3 Division of Advanced Materials Science, Pohang University of Science and Technology, Pohang, 790-784 (Republic of Korea)
‡ These authors contributed equally to this work.
* Corresponding authors
Abstract
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.
Keywords: aggregation; β-amyloid; cucurbit[7]uril; insulin; supramolecular chemistry
논문정보
- Research article
- 2014년 05월 (BRIC 등록일 2014-05-23)
- 국내 연구진
- 생명과학 > 생화학
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