Issue 55, 2016
From the journal:

Chemical Communications

Nanoscale insights into full-length prion protein aggregation on model lipid membranes†

Yangang Pan,a   Bin Wang,a   Tong Zhang,a   Yanan Zhang,a   Hongda Wangb  and  Bingqian Xu*a  

* Corresponding authors

a Single Molecule Study Laboratory, Faculty of Engineering and Nanoscale Science and Engineering Center, University of Georgia, Athens, GA 30602, USA
E-mail: bxu@engr.uga.edu

b State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022, P. R. China

Abstract

The aggregates of the full-length human recombinant prion protein (PrP) (23–231) on model membranes were investigated by combining the atomic force microscopy (AFM) measurements and theoretical calculations at pH 5.0, showing the great effect of PrP concentration on its supramolecular assemblies on the lipid bilayer.

Graphical abstract: Nanoscale insights into full-length prion protein aggregation on model lipid membranes

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Article information

DOI
https://doi.org/10.1039/C6CC03029G
Article type
Communication
Submitted
11 Apr 2016
Accepted
30 May 2016
First published
31 May 2016

Chem. Commun., 2016,52, 8533-8536

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Nanoscale insights into full-length prion protein aggregation on model lipid membranes

Y. Pan, B. Wang, T. Zhang, Y. Zhang, H. Wang and B. Xu, Chem. Commun., 2016, 52, 8533 DOI: 10.1039/C6CC03029G

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