Issue 100, 2012
From the journal:

Chemical Communications

Structural basis of single molecular heparin–FX06 interaction revealed by SPM measurements and molecular simulations†

Cunlan Guo,a   Bin Wang,a   Lianchun Wangb  and  Bingqian Xu*a  

* Corresponding authors

a Single Molecule Study Laboratory, College 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 Complex Carbohydrate Research Center and Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA

Abstract

Heparin, a functionalized polysaccharide, is observed under a scanning tunneling microscope, which shows atomic scale conformational details. The peptide FX06 is found to bind to five consecutive sugar units of heparin and this interaction is directly revealed by atomic force microscopy and dynamic force spectroscopy measurements. The determined free energy change agrees well with the dynamic calculation result.

Graphical abstract: Structural basis of single molecular heparin–FX06 interaction revealed by SPM measurements and molecular simulations

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Article information

DOI
https://doi.org/10.1039/C2CC36546D
Article type
Communication
Submitted
08 Sep 2012
Accepted
01 Nov 2012
First published
02 Nov 2012

Chem. Commun., 2012,48, 12222-12224

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Structural basis of single molecular heparin–FX06 interaction revealed by SPM measurements and molecular simulations

C. Guo, B. Wang, L. Wang and B. Xu, Chem. Commun., 2012, 48, 12222 DOI: 10.1039/C2CC36546D

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