Abstract
 
Vol 49 No. 4: 355-360 [PDF] [Full Text]
 
The effect of aluminum ion on the aggregation of human islet amyloid polypeptide (11-28)
 
Lanlan Su1, Cheng Lu1, Peng Yan1, Nan Zhang1, Sheng Cai2, Gongjun Zhang2, Xingfei Zhou1,*, and Bin Li3,*

1School of Science, Ningbo University, Ningbo 315211, China,
2Ningbo Institute of Material Technology and Engineering, Chinese Academy of Sciences, Ningbo 315201, China, and
3Laboratory of Physical Biology, Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai 201800, China
 

Abstract  Metal ions play a critical role in human islet amyloid polypeptide (hIAPP) aggregation, which is believed to be closely associated with β-cell death in type II diabetes. In this work, the effect of Al3+ on the aggregation of hIAPP (11-28) was studied by several different experimental approaches. Atomic force microscopy measurements showed that Al3+ could remarkably inhibit hIAPP(11-28) fibrillogenesis, while Zn2+ had a slight promotion effect on peptide aggregation, which was also confirmed by Thioflavin T fluorescence observation. Furthermore, X-ray photoelectron spectroscopy measurement indicated that Al ions might form chemical bonds with neighboring atoms and destroy the secondary structures of the protein. Our studies could deepen the understanding of the role of metal ions in the aggregation of amyloid peptides.

 

Keywords   metal ion, hIAPP peptides, atomic force microscopy, Thioflavin T fluorescence, X-ray photoelectron spectroscopy

 

Received   2016-12-16  
Accepted  
2017-1-21

 

Funding  This work was supported by the National Natural Science Foundation of China (Nos. 1147417, 11375253, and 31670871), the Natural Science Foundation of Zhejiang Province (No. LY14A040002), and the K. C. Wong Magna Fund in Ningbo University.

 

* Correspondence address  Tel/Fax: +86-574-87600744; E-mail: zhouxingfei@nbu.edu.cn (X.Z.)/Tel: +86-215-9553998; Fax: +86-215-9552394; E-mail: Libin@sinap.ac.cn (B.L.)

 
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