Co-assembly of human islet amyloid polypeptide (hIAPP)/insulin

被引：45

作者：

Liu, Peng ^{[1
]}

Zhang, Shuai ^{[2
,3
]}

Chen, Mei-sha ^{[1
]}

Liu, Qian ^{[1
]}

Wang, Chenxuan ^{[4
]}

Wang, Chen ^{[4
]}

Li, Yan-Mei ^{[1
]}

Besenbacher, Flemming ^{[2
,3
]}

Dong, Mingdong ^{[2
,3
]}

机构：

[1] Tsinghua Univ, Key Lab Bioorgan Phosphorus Chem & Chem Biol, Minist Educ, Dept Chem, Beijing 100084, Peoples R China

[2] Aarhus Univ, Interdisciplinary Nanosci Ctr iNANO, DK-8000 Aarhus C, Denmark

[3] Aarhus Univ, Dept Phys & Astron, DK-8000 Aarhus C, Denmark

[4] Natl Ctr Nanosci & Technol, Beijing 100190, Peoples R China

来源：

CHEMICAL COMMUNICATIONS | 2012年 / 48卷 / 02期

基金：

中国国家自然科学基金;

关键词：

CONFORMATIONAL-CHANGES; INSULIN; PROTEIN; OLIGOMERS; MEMBRANE; MECHANISM; SPECTROSCOPY; APOPTOSIS; TYPE-2;

D O I：

10.1039/c1cc14285b

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The pathogenesis of type II diabetes can be linked to cosecreted hIAPP/insulin interacting with cell membranes. Here we investigate the nanostructures by co-assembling hIAPP and insulin on surfaces. By tuning the hIAPP/insulin ratio, atomic force microscopy reveals the resulting nanostructure morphology changes from fibrils to oligomers, to annular. Implications for in vivo studies are discussed.

引用

页码：191 / 193

页数：3

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