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Does the fluorescence quencher acrylamide bind to proteins?

M R Eftink¹, C A Ghiron

¹Department of Chemistry, University of Mississippi, University 38677.

Biochimica Et Biophysica Acta

|December 18, 1987

Summary

This study found no protein concentration dependence in acrylamide quenching of protein fluorescence, suggesting weak acrylamide-protein interactions, contrary to prior reports.

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Area of Science:

Biochemistry
Biophysics
Protein Chemistry

Background:

Acrylamide quenching of protein fluorescence is a method used to study protein structure and interactions.
Previous studies suggested strong interactions between acrylamide and proteins, but this was not consistently observed.

Purpose of the Study:

To investigate the protein concentration dependence of acrylamide quenching on protein fluorescence.
To evaluate the extent of acrylamide-protein interactions using fluorescence lifetime measurements and equilibrium dialysis.

Main Methods:

Fluorescence lifetime measurements using phase/modulation fluorometry.
Equilibrium dialysis to assess acrylamide-serum albumin association.
Enzyme activity assays to determine acrylamide's effect on protein function.

Main Results:

No protein concentration dependence was observed for acrylamide quenching of human serum albumin and monellin fluorescence across a 0.5-20 mg/ml concentration range.
Equilibrium dialysis revealed no significant association between acrylamide and serum albumin.
Acrylamide exhibited only a minor impact on the activity of selected enzymes.

Conclusions:

The findings suggest weak acrylamide-protein interactions, contradicting previous reports.
Acrylamide's effect on protein fluorescence and activity is minimal and not dependent on protein concentration within the studied range.

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