文献详情
Inhibitory effects of oxidovanadium complexes on the aggregation of human islet amyloid polypeptide and its fragments
文献类型:期刊
期刊名称:Journal of inorganic biochemistry影响因子和分区
年:2019
卷:197
页码:110721
ISSN:1873-3344
关键词:Aggregation,Inhibition,Oxidovanadium complexes,hIAPP,hIAPP19-37,hIAPP20-29
所属部门:化学系
摘要:Human islet amyloid polypeptide (hIAPP) is synthesized by pancreatic β-cells and co-secreted with insulin. Misfolding and amyloidosis of hIAPP induce β-cell dysfunction in type II diabetes mellitus. Numerous small organic molecules and metal complexes act as inhibitors against amyloid-related diseases, justifying the need to explore the inhibitory mechanism of these compounds. In this work, three oxidovanadium complexes, namely, (NH4)[VO(O2)2(bipy)]·4H2O (1) (bipy?=?2,2' bipyridine), bis(ethyl-m ...More
Human islet amyloid polypeptide (hIAPP) is synthesized by pancreatic β-cells and co-secreted with insulin. Misfolding and amyloidosis of hIAPP induce β-cell dysfunction in type II diabetes mellitus. Numerous small organic molecules and metal complexes act as inhibitors against amyloid-related diseases, justifying the need to explore the inhibitory mechanism of these compounds. In this work, three oxidovanadium complexes, namely, (NH4)[VO(O2)2(bipy)]·4H2O (1) (bipy?=?2,2' bipyridine), bis(ethyl-maltolato, O,O)oxido-vanadium(IV) (2), and (bipyH2)H2[O{VO(O2)(bipy)}2]·5H2O (3), were synthesized and used to inhibit the aggregation of hIAPP and its fragments, namely, hIAPP19-37 and hIAPP20-29. Results revealed that shortening the peptide sequence decreased the aggregation capability of hIAPP fragments, and the oxidovanadium complexes inhibited the fibrillization of hIAPP better than its fragments. Interestingly, the binding of oxidovanadium complexes to hIAPP and its fragments presented a distinct thermodynamic behavior. Oxidovanadium complexes featured the disaggregation capability against hIAPP, better than against its fragments. These complexes also decreased the cytotoxicity caused by hIAPP and its fragments by reducing the production of oligomers. 3 may be a good hIAPP inhibitor based on its inhibition, disaggregation capability, and regulatory effect on peptide-induced cytotoxicity. Oxidovanadium complexes exhibit potential as metallodrugs against amyloidosis-related diseases.Copyright ? 2019 Elsevier Inc. All rights reserved. ...Hide
DOI:10.1016/j.jinorgbio.2019.110721
百度学术:Inhibitory effects of oxidovanadium complexes on the aggregation of human islet amyloid polypeptide and its fragments
语言:外文
人气指数:2
浏览次数:2
作者其他论文
Influence of methionine-ruthenium complex on the fibril formation of human islet amyloid polypeptide.Gong Gehui, Xu Jufei, Huang Xiangyi, et al. .Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 2019, 24(2), 179-189.
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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Inhibitory effects of oxidovanadium complexes on the aggregation of human islet amyloid polypeptide
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