Issue 11, 2012
From the journal:

Chemical Communications

Following aptamer–ricin specific binding by single molecule recognition and force spectroscopy measurements†

Bin Wang,a   Cunlan Guo,a   Guojun Chen,a   Bosoon Parkb  and  Bingqian Xu*a  

* Corresponding authors

a Single Molecule Study Laboratory, Faculty of Engineering and Nanoscale Science and Engineering Center, University of Georgia, Athens, USA
E-mail: bxu@engr.uga.edu
Fax: +1-706-542-3804
Tel: +1-706-542-0502

b USDA-ARS, Russell Research Center, Athens, USA

Abstract

Single molecule recognition imaging and dynamic force spectroscopy (DFS) analysis showed strong binding affinity between an aptamer and ricin, which was comparable with antibody–ricin interaction. Molecular simulation showed a ricin binding conformation with aptamers and gave different ricin conformations immobilizing on substrates that were consistent with AFM images.

Graphical abstract: Following aptamer–ricin specific binding by single molecule recognition and force spectroscopy measurements

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Article information

DOI
https://doi.org/10.1039/C1CC15644F
Article type
Communication
Submitted
12 Sep 2011
Accepted
30 Oct 2011
First published
11 Nov 2011

Chem. Commun., 2012,48, 1644-1646

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Following aptamer–ricin specific binding by single molecule recognition and force spectroscopy measurements

B. Wang, C. Guo, G. Chen, B. Park and B. Xu, Chem. Commun., 2012, 48, 1644 DOI: 10.1039/C1CC15644F

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