%0 Journal Article %A CHEN Wuchao %A LI Lin %A LU Cheng %A YAN Peng %A ZHANG Gongjun %A ZHANG Nan %A ZHOU Xingfei %T Effect of Copper Ions on the Aggregation of Human Islet Amyloid Polypeptide(1128) %D 2018 %R 10.11944/j.issn.1000-0518.2018.02.170378 %J Chinese Journal of Applied Chemistry %P 147-153 %V 35 %N 2 %X

Human islet amyloid polypeptide(hIAPP) is closely associated with type 2 diabetes mellitus(T2DM), which is one of possible pathogenic factors of islet beta cell apoptosis. It has been suggested that the environmental factors(such as metal ions, pH and temperature) have great effects on the aggregation process of hIAPP. In this study, we investigate the influence of copper(Ⅱ) ions on the aggregation of hIAPP and its fragments by a variety of biophysical methods. Atomic force microscope(AFM) and thioflavin T(ThT) fluorescence measurements show that the copper ions can inhibit hIAPP(137) and hIAPP(1128) to aggregate into fibers. In addition, the micro-Fourier transform infrared spectroscopy(Micro-FTIR) shows that copper ions can restrain the transition from alpha helices structure to beta sheets formation during the peptide incubation. By the single amino acid mutation experiment, we speculate that the His18 in hIAPP(1128) may have a dominant effect on the aggregation behavior and the interaction with copper ions.

%U http://yyhx.ciac.jl.cn/EN/10.11944/j.issn.1000-0518.2018.02.170378