Issue 5, 2011
From the journal:

Chemical Communications

The binding of CNA35 contrast agents to collagen fibrils†

Honorius M. H. F. Sanders,a   Michele Iafisco,bc   Emilie M. Pouget,d   Paul H. H. Bomans,d   Fabio Nudelman,d   Giuseppe Falini,b   Gijsbertus de With,d   Maarten Merkx,e   Gustav J. Strijkers,a   Klaas Nicolay*a  and  Nico A. J. M. Sommerdijk*d  

* Corresponding authors

a Biomedical NMR, Department of Biomedical Engineering, Eindhoven University of Technology, P.O. Box 513, 5600 MB Eindhoven, The Netherlands
E-mail: k.nicolay@tue.nl

b Dipartimento di Chimica “G. Ciamician”, Alma Mater Studiorum Università di Bologna, Via Selmi 2, 40126 Bologna, Italy

c Dipartimento di Scienze Mediche, Università del Piemonte Orientale, Via Solaroli 4, 28100 Novara, Italy

d Laboratory of Materials and Interface Chemistry and Soft Matter CryoTEM Research Unit, Department of Chemical Engineering and Chemistry, Eindhoven University of Technology, The Netherlands

e Laboratory of Chemical Biology, Department of Biomedical Engineering, Eindhoven University of Technology, The Netherlands
E-mail: n.a.j.m.sommerdijk@tue.nl

Abstract

CryoTEM demonstrates that a CNA35-bearing liposomal MRI contrast agent selectively binds to poorly assembled collagen type I as opposed to well-assembled collagen fibrils, whereas monomeric CNA35 binds to all forms of collagen. It is shown that upon conjugation to liposomes and micelles CNA35 loses its ability to dissociate ordered collagen fibrils and thereby to create its own binding sites.

Graphical abstract: The binding of CNA35 contrast agents to collagen fibrils

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Article information

DOI
https://doi.org/10.1039/C0CC02901G
Article type
Communication
Submitted
29 Jul 2010
Accepted
28 Oct 2010
First published
18 Nov 2010

Chem. Commun., 2011,47, 1503-1505

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The binding of CNA35 contrast agents to collagen fibrils

H. M. H. F. Sanders, M. Iafisco, E. M. Pouget, P. H. H. Bomans, F. Nudelman, G. Falini, G. de With, M. Merkx, G. J. Strijkers, K. Nicolay and N. A. J. M. Sommerdijk, Chem. Commun., 2011, 47, 1503 DOI: 10.1039/C0CC02901G

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