Citation: LU Cheng, LI Lin, YAN Peng, ZHANG Nan, CHEN Wuchao, ZHANG Gongjun, ZHOU Xingfei. Effect of Copper Ions on the Aggregation of Human Islet Amyloid Polypeptide(11~28)[J]. Chinese Journal of Applied Chemistry, ;2018, 35(2): 147-153. doi: 10.11944/j.issn.1000-0518.2018.02.170378 shu

Effect of Copper Ions on the Aggregation of Human Islet Amyloid Polypeptide(11~28)

LU Cheng ^a ,
LI Lin ^a ,
YAN Peng ^a ,
ZHANG Nan ^a ,
CHEN Wuchao ^a ,
ZHANG Gongjun ^b ,
ZHOU Xingfei ^a,,

a.
School of Science, Ningbo University, Ningbo, Zhejiang 315211, China
b.
Ningbo Institute of Material Technology and Engineering, Chinese Academy of Sciences, Ningbo, Zhejiang 315201, China

Corresponding author: ZHOU Xingfei, zhouxingfei@nbu.edu.cn
Received Date: 23 October 2017
Revised Date: 29 November 2017
Accepted Date: 18 December 2017

Fund Project: Supported by the National Natural Science Foundation of China(No.11474173), the Zhejiang Provincial Natural Science Foundation(No.LY18A040003)the National Natural Science Foundation of China 11474173the Zhejiang Provincial Natural Science Foundation LY18A040003

Figures(6)

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(1~37) and hIAPP(11~28) 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(11~28) may have a dominant effect on the aggregation behavior and the interaction with copper ions.
- copper(Ⅱ) ions,
- human islet amyloid protein,
- type 2 diabetes
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