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Pluronic additives: a solution to sticky problems in digital microfluidics.

Vivienne N Luk¹, Gary Ch Mo, Aaron R Wheeler

¹Department of Chemistry, University of Toronto, 80 St. George Street, Toronto, Ontario M5S 3H6, Canada.

Langmuir : the ACS Journal of Surfaces and Colloids

|May 17, 2008

Summary

This summary is machine-generated.

Researchers found that adding Pluronic F127 to digital microfluidics (DMF) solutions significantly reduces protein adsorption. This breakthrough enables higher protein concentrations in DMF assays, overcoming a major limitation for the technology.

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Area of Science:

Biotechnology
Microfluidics
Surface Chemistry

Background:

Digital microfluidics (DMF) enables automated biochemical assays using microdroplets.
Nonspecific protein adsorption to device surfaces is a key limitation in DMF, affecting assay accuracy and droplet movement.

Purpose of the Study:

To quantitatively analyze protein adsorption on DMF devices.
To develop an effective method to mitigate protein adsorption in DMF.

Main Methods:

Confocal microscopy was used to analyze protein adsorption.
Secondary ion mass spectrometry provided quantitative adsorption data.
Experiments involved testing Pluronic F127 as a solution additive.

Main Results:

Low concentrations of Pluronic F127 effectively limit protein adsorption on DMF surfaces.
The additive allows for over 1000-fold higher protein concentrations in droplets.
A DMF-based protein digest assay demonstrated successful implementation with high protein concentrations (1 mg/mL).

Conclusions:

Pluronic F127 is a simple and effective solution to reduce protein adsorption in DMF.
This method significantly enhances the capabilities and applications of digital microfluidics.
The technology is now compatible with a wider range of biochemical assays involving high protein concentrations.