Issue 8, 2011
From the journal:

Nanoscale

Assembly of glucagon (proto)fibrils by longitudinal addition of oligomers†

Xingfei Zhou,*a   Jingsong Liu,a   Bin Li,b   Saju Pillai,c   Dongdong Lin,a   Jianhua Liua  and  Yi Zhang*b  

* Corresponding authors

a Physical Department, Ningbo University, Ningbo Zhejiang, China
E-mail: zhouxingfei@nbu.edu.cn
Tel: +86-574-87609970

b Laboratory of Physical Biology, Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai, China
E-mail: zhangyi@sinap.ac.cn
Fax: +86-21-59552394
Tel: +86-21-39194607

c Department of Mechanical Engineering, Aalborg University, Denmark

Abstract

The process of glucagon peptide aggregation was studied with high resolution atomic force microscopy (AFM). The statistical analysis of ex situAFM images in combination with in situAFM observation suggests that it is more likely that (proto)fibrils are formed via direct longitudinal growth of oligomers, instead of the lateral association of two or more filaments.

Graphical abstract: Assembly of glucagon (proto)fibrils by longitudinal addition of oligomers

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Article information

DOI
https://doi.org/10.1039/C1NR10332F
Article type
Communication
Submitted
29 Mar 2011
Accepted
13 May 2011
First published
04 Jul 2011

Nanoscale, 2011,3, 3049-3051

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Assembly of glucagon (proto)fibrils by longitudinal addition of oligomers

X. Zhou, J. Liu, B. Li, S. Pillai, D. Lin, J. Liu and Y. Zhang, Nanoscale, 2011, 3, 3049 DOI: 10.1039/C1NR10332F

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