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Detection of Protein Aggregation using Fluorescence Correlation Spectroscopy
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Fluorescence turn on by cholate aggregates.

Anthony Baldridge1, Adrian Amador, Laren M Tolbert

  • 1School of Chemistry and Biochemistry, 901 Atlantic Drive, Georgia Institute of Technology, Atlanta, Georgia 30332-0400, United States.

Langmuir : the ACS Journal of Surfaces and Colloids
|March 15, 2011
PubMed
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Bile salt aggregates, like sodium cholate, can bind and activate fluorescent protein analogs. This discovery may lead to new methods for studying biological transport systems.

Area of Science:

  • Biochemistry
  • Supramolecular Chemistry
  • Cell Biology

Background:

  • Bile salts, such as sodium cholate (NaCh), are amphiphilic molecules crucial for biological processes.
  • They form aggregates in aqueous solutions, aiding in the solubilization and transport of cholesterol, lipids, and vitamins.
  • Previous work demonstrated encapsulation of fluorescent protein (FP) analogs by synthetic hosts.

Purpose of the Study:

  • To investigate the binding and activation of fluorescent protein analogs by bile salt aggregates.
  • To explore the potential of bile salt systems as novel tools for biological trafficking studies.

Main Methods:

  • Formation of bile salt aggregates in aqueous solutions.
  • Incubation of fluorescent protein analogs with bile salt aggregates.

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  • Observation and analysis of binding and fluorescence changes.

    • Main Results:

    • Bile salt aggregates successfully bound to tested fluorescent protein analogs.
    • The binding event resulted in a "turn on" of fluorescence for these analogs.
    • This interaction demonstrates a new host-guest system involving natural surfactants.

    Conclusions:

    • Bile salt aggregates can serve as hosts for fluorescent protein analogs.
    • This interaction leads to fluorescence activation, offering a potential signaling mechanism.
    • These findings may pave the way for developing new tools to study biological trafficking.