文献详情
Influence of methionine-ruthenium complex on the fibril formation of human islet amyloid polypeptide
文献类型:期刊
通讯作者:Du, WH (reprint author), Renmin Univ China, Dept Chem, Beijing 100872, Peoples R China.
期刊名称:JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY影响因子和分区
年:2019
卷:24
期:2
页码:179-189
ISSN:0949-8257
关键词:hIAPP; Fibril formation; Ruthenium complexes; Inhibition
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)3H(2)O (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) ...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)3H(2)O (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)]Cl-2(2) and Ru(bipy)(2)Cl-2(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. Graphical abstract Methionine-Ru complex effectively impedes the fibril formation of human islet amyloid polypeptide. [GRAPHICS] . ...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
被引频次:2
基金:National Natural Science Foundation of ChinaNational Natural Science Foundation of China [21473251, 21271185]
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.
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.
Assembly behavior of amylin fragment hIAPP19-37 regulated by Au(III) complexes.Huang, Xiangyi, Xu, Jufei, Du, Weihong,.JOURNAL OF INORGANIC BIOCHEMISTRY. 2019, 201.
Regulation of Artemisinin and Its Derivatives on the Assembly Behavior and Cytotoxicity of Amyloid Polypeptides hIAPP and A beta.Xu, Jufei, Zhao, Cong, Huang, Xiangyi, et al. .ACS CHEMICAL NEUROSCIENCE. 2019, 10(11), 4522-4534.
Inhibitory effects of NAMI-A-like ruthenium complexes on prion neuropeptide fibril formation.Wang, Xuesong;Zhu, Dengsen;Zhao, Cong,等.METALLOMICS.2015,7(5),837-846.
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Influence of methionine-ruthenium complex on the fibril formation of human islet amyloid polypepti
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