Supramolecular Inhibition of Amyloid Fibrillation by Cucurbit[7]uril
| Autor: | Jong Wha Lee, Hugh I. Kim, Shin Jung C. Lee, Young Ho Ko, Tae Su Choi, Won Jong Kim, Junghong Park, Kimoon Kim, Hong Hee Lee |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
Bridged-Ring Compounds
Amyloid Stereochemistry Molecular Sequence Data Supramolecular chemistry Phenylalanine macromolecular substances Catalysis Hydrophobic effect chemistry.chemical_compound Cell Line Tumor mental disorders medicine Humans Amino Acid Sequence Therapeutic strategy Fibrillation Amyloid beta-Peptides Amyloidosis Imidazoles General Chemistry General Medicine medicine.disease Monomer chemistry medicine.symptom |
| Zdroj: | Angewandte Chemie. 126:7591-7595 |
| ISSN: | 0044-8249 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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