Supramolecular inhibition of amyloid fibrillation by cucurbit[7]uril

Hong Hee Lee, Tae Su Choi, Shin Jung C. Lee, Jong Wha Lee, Junghong Park, Young Ho Ko, Won Jong Kim, Kimoon Kim, Hugh I. Kim

Research output: Contribution to journalArticle

80 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)7461-7465
Number of pages5
JournalAngewandte Chemie - International Edition
Issue number29
Publication statusPublished - 2014 Jul 14
Externally publishedYes


  • aggregation
  • cucurbit[7]uril
  • insulin
  • supramolecular chemistry
  • β-amyloid

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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  • Cite this

    Lee, H. H., Choi, T. S., Lee, S. J. C., Lee, J. W., Park, J., Ko, Y. H., Kim, W. J., Kim, K., & Kim, H. I. (2014). Supramolecular inhibition of amyloid fibrillation by cucurbit[7]uril. Angewandte Chemie - International Edition, 53(29), 7461-7465.