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Ultralow interfacial tensions of aqueous two-phase systems measured using drop shape
Ehsan Atefi1, J Adin Mann, Hossein Tavana
1Department of Biomedical Engineering, The University of Akron , Akron, Ohio 44325, United States.
This study precisely measures ultralow interfacial tensions in polymer-based aqueous two-phase systems (ATPS) using axisymmetric drop shape analysis. These reproducible measurements are crucial for understanding biomolecule partitioning in ATPS.
Area of Science:
- Biophysical Chemistry
- Separation Science
- Materials Science
Background:
- Aqueous two-phase systems (ATPS) offer a biocompatible environment for biomolecule separation.
- Interfacial tension is critical for biomolecule partitioning in ATPS but challenging to measure due to ultralow values.
- Existing methods lack reproducibility for determining these subtle interfacial forces.
Purpose of the Study:
- To develop and validate a precise method for measuring ultralow interfacial tensions in polymeric ATPS.
- To systematically investigate interfacial tensions in polyethylene glycol (PEG)/dextran (DEX) ATPS.
- To establish reproducible experimental criteria for interfacial tension determination.
Main Methods:
- Utilized sessile and pendant drop techniques with axisymmetric drop shape analysis (ADSA).
- Studied eight different ATPS formulations composed of PEG and DEX.
- Implemented specific criteria for reproducible measurement of ultralow interfacial tensions.
Main Results:
- Achieved high reproducibility, with pendant and sessile drop methods yielding results within 0.001 mJ/m(2) of each other.
- Measured interfacial tensions ranging from 0.012 ± 0.001 mJ/m(2) to 0.381 ± 0.006 mJ/m(2).
- Demonstrated that interfacial tension varies with polymer concentrations in the ATPS phases.
Conclusions:
- The developed ADSA method provides reliable and reproducible measurements of ultralow interfacial tensions in ATPS.
- Accurate interfacial tension data is essential for optimizing ATPS applications in biomolecule separation and analysis.
- These findings will advance the understanding of biomolecule behavior and partitioning within ATPS.
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