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Issue 3, 2008
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Structure of cytochrome c at the interface with magnetic CoFe2O4nanoparticles

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Abstract

Yeast and horse cytochrome c are attached to 6 nm CoFe2O4nanoparticles and their structure is studied as a function of the nanoparticle surface chemistry. For yeast cytochrome c, the attachment is covalent and site-specific via dithiol cross-linkage between cysteine 102 and dimercaptosuccinic acid, the nanoparticle ligand. To control site-specificity and allow better characterization of non-specific interactions, horse cytochrome c is non-specifically linked to the nanoparticle. Circular dichroism shows that the structure of both proteins is affected by linkage to the CoFe2O4nanoparticle. Non-specific adsorption depends strongly on the surface properties of the nanoparticles. Co-functionalization with lysine improves protein folding, most likely by decreasing the nanoparticle net charge and impeding carboxylic acids residues from binding to surface cobalt and iron atoms. Higher protein coverage also helps folding for both yeast and horse cytochrome c.

Graphical abstract: Structure of cytochrome c at the interface with magnetic CoFe2O4nanoparticles

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Supplementary files

Article information


Submitted
03 Aug 2007
Accepted
14 Nov 2007
First published
10 Jan 2008

Soft Matter, 2008,4, 554-559
Article type
Paper

Structure of cytochrome c at the interface with magnetic CoFe2O4nanoparticles

M. Aubin-Tam, H. Zhou and K. Hamad-Schifferli, Soft Matter, 2008, 4, 554
DOI: 10.1039/B711937B

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