한빛사 논문
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
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