| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5152616 | Journal of Inorganic Biochemistry | 2017 | 43 Pages |
Abstract
Two tetracoordinated gold-sulfur complexes inhibit the aggregation of prion neuropeptide PrP106-126 and human islet amyloid polypeptide via metal coordination and hydrophobic interaction. The two complexes may scatter the peptides into nano scale particles and effectively upregulate the cell viability affected by the peptides.74
Keywords
DLSdiethyl dithiocarbamate3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyltetrazolium bromideDDTCTOCSYT2DMhIAPPPrPAβPDTESI-MSnuclear magnetic resonanceDMSOMTTInteractionElectrospray Ionization Mass SpectrometryTemInhibitionThTAggregationNMRThioflavin THISpyrrolidine dithiocarbamatedimethyl sulphoxideType 2 diabetes mellitusTotal correlation spectroscopyMethionineMETTransmission electron microscopyhistidineDynamic Light Scatteringamyloid-β proteinPrion proteinhuman islet amyloid polypeptideAmyloid peptides
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Wenji Wang, Cong Zhao, Dengsen Zhu, Gehui Gong, Weihong Du,