| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5152365 | Journal of Inorganic Biochemistry | 2017 | 38 Pages |
Abstract
Ruthemium polypyridyl complexes disaggregate the fibrils of human islet amyloid polypeptide into nano scale particles through hydrophobic interaction and metal coordination, and decrease the peptide induced cytotoxicity. The binding is an exothermic process with increased entropy effect.62
Keywords
AFMdpqPBSdppzbpyPrP106-126hIAPPESI-MST2DITCnuclear magnetic resonance1,10-Phenanthroline2,2′-BipyridineMTTROSInteractionElectrospray Ionization Mass SpectrometryTemThTDisaggregationNMRTyrTyrosineThioflavine TType II diabetesphosphate buffer salinePhenTransmission electron microscopeAtomic Force MicroscopeIsothermal titration calorimetryReactive oxygen species
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Dengsen Zhu, Gehui Gong, Wenji Wang, Weihong Du,