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

Authors

Xingfei Zhou, Ningbo University
Jingsong Liu, Ningbo University
Bin Li, Shanghai Institute of Applied Physics, Chinese Academy of Sciences
Saju Pillai, Aalborg University
Dongdong Lin, Ningbo University
Jianhua Liu, Ningbo University
Yi Zhang, Shanghai Institute of Applied Physics, Chinese Academy of Sciences

Document Type

Article

Publication Date

8-1-2011

Abstract

The process of glucagon peptide aggregation was studied with high resolution atomic force microscopy (AFM). The statistical analysis of ex situ AFM images in combination with in situ AFM 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. © 2011 The Royal Society of Chemistry.

Publication Source (Journal or Book title)

Nanoscale

First Page

3049

Last Page

3051

Recommended Citation

Zhou, X., Liu, J., Li, B., Pillai, S., Lin, D., Liu, J., & Zhang, Y. (2011). Assembly of glucagon (proto)fibrils by longitudinal addition of oligomers. Nanoscale, 3 (8), 3049-3051. https://doi.org/10.1039/c1nr10332f