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

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 det...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2012-01, Vol.48 (48), p.6037-6039
Main Authors: Basit, Hajra, Shivaji Sharma, K, Van der Heyden, Angéline, Gondran, Chantal, Breyton, Cécile, Dumy, Pascal, Winnik, Françoise M, Labbé, Pierre
Format: Article
Language:English
Subjects:
Bacteria
Bacterial Outer Membrane Proteins - chemistry
Bacterial Outer Membrane Proteins - metabolism
Bacteriophages - chemistry
Bacteriophages - metabolism
Binding Sites
Chemical communication
Chemical Sciences
Escherichia coli - chemistry
Escherichia coli - metabolism
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - metabolism
T-Phages - chemistry
T-Phages - metabolism
Viral Proteins - chemistry
Viral Proteins - metabolism
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Summary: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.
ISSN:1359-7345
1364-548X
DOI:10.1039/c2cc31107k