Issue 11, 2015
From the journal:

Chemical Communications

Following the aggregation of human prion protein on Au(111) surface in real-time†

Bin Wang,a   Cunlan Guo,ab   Zhichao Louac  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
Fax: +1-706-542-3804
Tel: +1-706-542-0502

b Departments of Materials and Interfaces, Weizmann Institute of Science, POB 26, Rehovot, Israel

c College of Materials Science and Technology, Nanjing University of Aeronautics and Astronautics, Nanjing, P. R. China

Abstract

Aggregations of human prion protein (23–231) were monitored by atomic force microscopy in real-time under pH 4. Prion dimers and trimers were determined as the basic units by AFM images and simulated structures. Aggregates aligned with the herringbone structures of an Au(111) reconstructed surface via Au–S bonds as the first layer, while the second layer was formed by non-covalent interactions.

Graphical abstract: Following the aggregation of human prion protein on Au(111) surface in real-time

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Article information

DOI
https://doi.org/10.1039/C4CC09209K
Article type
Communication
Submitted
18 Nov 2014
Accepted
08 Dec 2014
First published
08 Dec 2014

Chem. Commun., 2015,51, 2088-2090

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Following the aggregation of human prion protein on Au(111) surface in real-time

B. Wang, C. Guo, Z. Lou and B. Xu, Chem. Commun., 2015, 51, 2088 DOI: 10.1039/C4CC09209K

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