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

Chem Commun (Camb). 2012 Jun 18;48(48):6037-9. doi: 10.1039/c2cc31107k. Epub 2012 May 11.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Outer Membrane Proteins / chemistry*
  • Bacterial Outer Membrane Proteins / metabolism*
  • Bacteriophages / chemistry*
  • Bacteriophages / metabolism*
  • Binding Sites
  • 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*

Substances

  • Bacterial Outer Membrane Proteins
  • Escherichia coli Proteins
  • FhuA protein, E coli
  • Viral Proteins