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A Printed Equilibrium Dialysis Device with Integrated Membranes for Improved Binding Affinity Measurements
Cody W Pinger1, Andrew A Heller1, Dana M Spence1
1Department of Chemistry, ‡Department of Biomedical Engineering, and §Institute for Quantitative Health Science and Engineering, Michigan State University , 775 Woodlot Dr., East Lansing, Michigan 48824, United States.
Analytical Chemistry
|June 27, 2017
Summary
A 3D-printed device enables customizable equilibrium dialysis for protein-ligand binding studies. This novel approach accurately measures binding constants, like for Zn2+ and human serum albumin, using a 96-well plate format.
Area of Science:
- Biochemistry
- Analytical Chemistry
- Materials Science
Background:
- Equilibrium dialysis is a standard method for studying protein-ligand interactions.
- Existing methods can be limited in customization and throughput.
- There is a need for adaptable and high-throughput binding assay technologies.
Purpose of the Study:
- To develop and validate a 3D-printed device for equilibrium dialysis.
- To enable customizable membrane selection for specific experimental needs.
- To assess the device's performance in measuring protein-ion binding constants.
Main Methods:
- Fabrication of a 96-well plate-compatible equilibrium dialysis device using a 3D printer.
- Integration of regenerated-cellulose membranes (MWCO ~3500 Da) via a print-pause-print technique.
- Characterization of equilibrium attainment and measurement of Zn2+-human serum albumin binding constants.
Main Results:
- The 3D-printed device successfully integrated leak-free membranes.
- The device is compatible with automated liquid handling systems.
- Accurate measurement of the dissociation constant for Zn2+ and human serum albumin (Kd = (5.62 ± 0.93) × 10-7 M) was achieved.
Conclusions:
- 3D printing offers a versatile platform for creating customized equilibrium dialysis devices.
- The developed device provides a reliable and adaptable tool for biochemical binding studies.
- This technology facilitates high-throughput analysis of protein-ligand interactions under physiological conditions.
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