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Influence of methionine-ruthenium complex on the fibril formation of human islet amyloid polypeptide

本站小编 Free考研/2020-04-17

文献详情
Influence of methionine-ruthenium complex on the fibril formation of human islet amyloid polypeptide
文献类型:期刊
期刊名称:Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
年:2019
卷:24
期:2
页码:179-189
ISSN:1432-1327
关键词:Fibril formation,Inhibition,Ruthenium complexes,hIAPP
所属部门:化学系
摘要:The abnormal aggregation and deposition of human islet amyloid polypeptide (hIAPP) are implicated in the pathogeny of type 2 diabetes mellitus (T2DM). Many aromatic ring-containing Ru complexes inhibit the aggregation of hIAPP. A new Ru complex Ru(bipy)(met)2·3H2O (1), where bipy is 2,2'-bipyridine and met is methionine, was synthesized and employed to resist the fibril formation of hIAPP and to promote the biocompatibility of metal complexes. Two polypyridyl Ru complexes, namely [Ru(bipy)3]Cl2( ...More
The abnormal aggregation and deposition of human islet amyloid polypeptide (hIAPP) are implicated in the pathogeny of type 2 diabetes mellitus (T2DM). Many aromatic ring-containing Ru complexes inhibit the aggregation of hIAPP. A new Ru complex Ru(bipy)(met)2·3H2O (1), where bipy is 2,2'-bipyridine and met is methionine, was synthesized and employed to resist the fibril formation of hIAPP and to promote the biocompatibility of metal complexes. Two polypyridyl Ru complexes, namely [Ru(bipy)3]Cl2(2) and Ru(bipy)2Cl2(3), were used for comparison. Results reveal that the three Ru complexes can inhibit hIAPP aggregation and depolymerize mature hIAPP fibrils. Interaction studies show that Ru complexes bind to hIAPP through metal coordination, hydrophobic interaction, and other intermolecular forces. The binding of the three compounds is spontaneous and exothermic. The compounds also rescue peptide-induced cytotoxicity to some extent. Similar to 3, the novel methionine-Ru complex 1 exhibits an enhanced inhibitory effect and binding affinity to hIAPP possibly because of the smaller steric hindrance and more profitable molecular configuration of 1 than those of 2. The newly designed amino acid-Ru complex may provide new insights into the treatment of T2DM and related amyloidosis diseases. Methionine-Ru complex effectively impedes the fibril formation of human islet amyloid polypeptide. ...Hide

DOI:10.1007/s00775-019-01637-6
百度学术:Influence of methionine-ruthenium complex on the fibril formation of human islet amyloid polypeptide
语言:外文
作者其他论文



Inhibitory effects of oxidovanadium complexes on the aggregation of human islet amyloid polypeptide and its fragments.Xu Jufei, Zhang Baohong, Gong Gehui, et al. .Journal of inorganic biochemistry. 2019, 197, 110721.
Regulation of Artemisinin and Its Derivatives on the Assembly Behavior and Cytotoxicity of Amyloid Polypeptides hIAPP and Aβ.Xu Jufei, Zhao Cong, Huang Xiangyi, et al. .ACS chemical neuroscience. 2019, 10(11), 4522-4534.
Assembly behavior of amylin fragment hIAPP19-37 regulated by Au(III) complexes.Huang Xiangyi, Xu Jufei, Du Weihong,.Journal of inorganic biochemistry. 2019, 201, 110807.
Top-Down Extraction of Silk Protein Nanofibers by Natural Deep Eutectic Solvents and Application in Dispersion of Multiwalled Carbon Nanotubes for Wearable Sensing.Tan Xingxing, Wang Yaqing, Du Weihong, et al. .ChemSusChem. 2020, 13(2), 321-327.
Regulation of the aggregation behavior of human islet amyloid polypeptide fragment by titanocene complexes.Du, Weihong;Gong, Gehui;Wang, Wenji,等.JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY.2017,22(7),1065-1074.

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