Issue 2, 2012
From the journal:

Chemical Communications

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

Peng Liu,†a   Shuai Zhang,†b   Mei-sha Chen,a   Qian Liu,a   Chenxuan Wang,c   Chen Wang,c   Yan-Mei Li,*a   Flemming Besenbacher*b  and  Mingdong Dong*b  

* Corresponding authors

a Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing, China
E-mail: liym@mail.tsinghua.edu.cn
Fax: +86 10 6278 1695
Tel: +86 10 6279 6197

b Interdisciplinary Nanoscience Center (iNANO) and Department of Physics and Astronomy, Aarhus University, Aarhus C, Denmark
E-mail: fbe@inano.au.dk, dong@inano.au.dk
Fax: +45 8942 3690
Tel: +45 8942 3702

c National Center for Nanoscience and Technology, Beijing, China

Abstract

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.

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

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Article information

DOI
https://doi.org/10.1039/C1CC14285B
Article type
Communication
Submitted
15 Jul 2011
Accepted
28 Sep 2011
First published
14 Oct 2011

Chem. Commun., 2012,48, 191-193

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

P. Liu, S. Zhang, M. Chen, Q. Liu, C. Wang, C. Wang, Y. Li, F. Besenbacher and M. Dong, Chem. Commun., 2012, 48, 191 DOI: 10.1039/C1CC14285B

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