期刊
JOURNAL OF INORGANIC BIOCHEMISTRY
卷 170, 期 -, 页码 109-116出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2017.02.008
关键词
hIAPP; Ru polypyridyl complex; Interaction; Disaggregation
资金
- National Natural Science Foundation of China [21473251, 21271185]
- Fundamental Research Funds for the Central Universities
- Research Fund of Renmin University of China (RUC) [15XNLQ04]
The toxicity of amyloid proteins is associated with many degenerative and systematic diseases. The aggregation of human islet amyloid polypeptide may induce pancreatic beta-cell death, which is linked to type II diabetes. Ruthenium complexes are inhibitors of various proteins and potential anticancer metallodrugs, which can also be used to disaggregate amyloid proteins. This work reported that several ruthenium polypyridyl complexes remarkably affected the peptide aggregation by predominant hydrophobic interaction and metal coordination, as reflected by thermodynamic parameters and mass spectrometry analysis. Morphology and particle size analysis showed that the amyloid fibrils were disaggregated from long fibrils into small nano particles. Addition of these complexes also decreased the cytotoxicity induced by the peptide. The results indicated that ruthenium polypyridyl complexes may be potential metallodrugs to treat amyloidosis. (C) 2017 Elsevier Inc. All rights reserved.
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