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J Am Chem Soc. 2005 Mar 30;127(12):4320-5.

Tuning the orientation of an antigen by adsorption onto nanostriped templates.

Author information

1
Unité de Physique et de Chimie des Hauts Polymères (POLY) and Research Center in Micro- and Nanoscopic Materials and Electronic Devices (CeRMiN), Université catholique de Louvain, Place Croix du Sud, 1, B-1348 Louvain-la-Neuve, Belgium.

Abstract

We investigate the adsorption of a globular protein (P.69 pertactin, also known as antigen 69k) on protein-repellent hydrophilic substrates bearing regularly spaced hydrophobic nanostripes, for stripe widths comprised between 20 and 160 nm. Protein adsorption is shown to be remarkably well-controlled by the templating substrates, with a near-to-perfect reproduction of stripes by the protein monolayer down to 20 nm width, except for a 5-10 nm broadening. However, whereas the ellipsoidal protein forms a dense monolayer with random orientation of its long axis for large stripe widths, it adsorbs in a predominantly side-on (flat-on) orientation for stripe widths below 50 nm, due to the easier reorientation (interfacial relaxation) of the proteins adsorbed at the edges of the stripes, which experience a decreased lateral interaction. These results show that protein confinement in regions of a size similar to their dimensions can be used to tune their orientation, which may be of interest for applications in high-density sensor devices.

PMID:
15783213
DOI:
10.1021/ja043656r
[Indexed for MEDLINE]

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