Issue 48, 2012
From the journal:

Chemical Communications

Amphipol mediated surface immobilization of FhuA: a platform for label-free detection of the bacteriophage protein pb5†

Hajra Basit,*a   K. Shivaji Sharma,b   Angéline Van der Heyden,*a   Chantal Gondran,a   Cécile Breyton,c   Pascal Dumy,a   Françoise M. Winnikb  and  Pierre Labbéa  

* Corresponding authors

a Département de Chimie Moléculaire, UMR CNRS 5250, Université Joseph Fourier, 38041 Grenoble cedex 9, France
E-mail: hajra.basit@ujf-grenoble.fr, angeline.van-der-heyden@ujf-grenoble.fr

b Department of Chemistry and Faculty of Pharmacy, University of Montréal, Succursale Centre Ville, Montréal, QC, Canada,

c UMR 5075, CEA, CNRS, Institut de Biologie Structurale, Université Joseph Fourier, 38027 Grenoble, France

Abstract

Biotinylated amphipol was used to entrap FhuA (an E. coli outer membrane protein) and immobilize the FhuA–amphipol complex on streptavidin surfaces. Using this assembly, we have successfully devised surface-based assays for studying the recognition of FhuA by pb5 (a bacteriophage T5 protein) and determination of the affinity constant.

Graphical abstract: Amphipol mediated surface immobilization of FhuA: a platform for label-free detection of the bacteriophage protein pb5

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Article information

DOI
https://doi.org/10.1039/C2CC31107K
Article type
Communication
Submitted
14 Feb 2012
Accepted
24 Apr 2012
First published
25 Apr 2012

Chem. Commun., 2012,48, 6037-6039

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Amphipol mediated surface immobilization of FhuA: a platform for label-free detection of the bacteriophage protein pb5

H. Basit, K. Shivaji Sharma, A. Van der Heyden, C. Gondran, C. Breyton, P. Dumy, F. M. Winnik and P. Labbé, Chem. Commun., 2012, 48, 6037 DOI: 10.1039/C2CC31107K

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