The effect of aluminum ion on the aggregation of human islet amyloid polypeptide (11-28)
文献类型:期刊论文
作者 | Su, LL; Lu, C; Yan, P; Zhang, N; Cai, S; Zhang, GJ; Zhou, XF; Li, B |
刊名 | ACTA BIOCHIMICA ET BIOPHYSICA SINICA
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出版日期 | 2017 |
卷号 | 49期号:4页码:355-360 |
关键词 | Metal Ion Hiapp Peptides Atomic Force Microscopy Thioflavin t Fluorescence X-ray Photoelectron Spectroscopy |
ISSN号 | 1672-9145 |
DOI | 10.1093/abbs/gmx015 |
文献子类 | 期刊论文 |
英文摘要 | Metal ions play a critical role in human islet amyloid polypeptide (hIAPP) aggregation, which is believed to be closely associated with beta-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. |
语种 | 英语 |
WOS记录号 | WOS:000398771900008 |
源URL | [http://ir.sinap.ac.cn/handle/331007/27472] ![]() |
专题 | 上海应用物理研究所_中科院上海应用物理研究所2011-2017年 |
推荐引用方式 GB/T 7714 | Su, LL,Lu, C,Yan, P,et al. The effect of aluminum ion on the aggregation of human islet amyloid polypeptide (11-28)[J]. ACTA BIOCHIMICA ET BIOPHYSICA SINICA,2017,49(4):355-360. |
APA | Su, LL.,Lu, C.,Yan, P.,Zhang, N.,Cai, S.,...&Li, B.(2017).The effect of aluminum ion on the aggregation of human islet amyloid polypeptide (11-28).ACTA BIOCHIMICA ET BIOPHYSICA SINICA,49(4),355-360. |
MLA | Su, LL,et al."The effect of aluminum ion on the aggregation of human islet amyloid polypeptide (11-28)".ACTA BIOCHIMICA ET BIOPHYSICA SINICA 49.4(2017):355-360. |
入库方式: OAI收割
来源:上海应用物理研究所
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