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Related Experiment Videos

Characterizing specific phage-protein interactions by fluorescence correlation spectroscopy.

John T Bahns1, Chin-Mei Liu, Liaohai Chen

  • 1Biosciences Division, Argonne National Laboratory, Argonne, IL 60439, USA.

Protein Science : a Publication of the Protein Society
|September 25, 2004
PubMed
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Fluorescence Correlation Spectroscopy analyzed phage-target interactions. Methods were developed to overcome challenges in measuring filamentous M13 phage interactions, enabling dissociation constant determination.

Area of Science:

  • Biophysics
  • Molecular Interactions
  • Spectroscopy

Background:

  • Phage display is a powerful tool for identifying high-affinity ligands.
  • Characterizing the binding kinetics of phage-displayed affinity reagents is crucial for their application.
  • Fluorescence Correlation Spectroscopy (FCS) offers a sensitive method for studying molecular interactions in solution.

Purpose of the Study:

  • To investigate the binding interactions of T7 and M13 phage particles displaying affinity reagents with their target molecules.
  • To determine dissociation constants using Fluorescence Correlation Spectroscopy (FCS).
  • To develop and present methods for overcoming challenges in FCS measurements of filamentous M13 phage.

Main Methods:

  • Utilizing Fluorescence Correlation Spectroscopy (FCS) to analyze fluorescence autocorrelation curves.

Related Experiment Videos

  • Characterizing diffusion times and relative component fractions in equilibrium binding reactions.
  • Adapting confocal optics, fitting procedures, and aggregate discrimination for M13 phage FCS measurements.

    • Main Results:

    • Dissociation constants were successfully deduced for phage-target interactions.
    • FCS characterization of icosahedral T7 phage systems was straightforward.
    • Specific methods were developed to address complexities in M13 phage FCS measurements due to size and aggregation.

    Conclusions:

    • FCS is a viable technique for quantifying phage-target binding affinities.
    • The developed methods enhance the applicability of FCS to filamentous phage systems.
    • This work facilitates the quantitative analysis of affinity reagents displayed on different phage types.