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Thermoresponsive Self-Assembled β-Cyclodextrin-Modified Surface for Blood Purification
Sa Liu1, Chunting Zhong2, Junjian Chen1
1School of Materials Science and Engineering, South China University of Technology, Guangzhou 510641, China.
ACS Biomaterials Science & Engineering
|January 12, 2021
Summary
Researchers developed a recyclable surface to remove bilirubin, a toxin in liver failure patients. This innovative blood purification method enhances detoxification and reduces costs by utilizing host-guest interactions and thermoresponsive properties for repeated use.
Area of Science:
- Biomaterials Science
- Surface Chemistry
- Biomedical Engineering
Background:
- Bilirubin (BR) is an endogenous toxin accumulating in liver failure.
- Current blood purification methods for bilirubin removal require improvement and cost reduction.
Purpose of the Study:
- To develop a recyclable model surface for efficient bilirubin removal.
- To investigate the host-guest interactions and thermoresponsive properties for detoxification and recyclability.
Main Methods:
- Self-assembly of adamantane (Ad) on a gold surface.
- Integration of β-cyclodextrin dimer (CDD) via host-guest interactions with Ad.
- Characterization using XPS, contact angle, AFM, and QCM-D.
- In vitro assays for protein adsorption, platelet adhesion, hemolysis, and cytotoxicity.
Main Results:
- The modified surface strongly adsorbed bilirubin via CDD-bilirubin host-guest interactions.
- Detoxification efficiency was improved 1.7 times compared to Ad-only surface.
- The surface demonstrated recyclability for at least 3 cycles using a thermoresponsive property (45 °C).
- The surface showed reduced plasma protein adsorption, low platelet adhesion, no hemolysis, and negligible cytotoxicity.
Conclusions:
- The developed recyclable surface effectively removes bilirubin using host-guest self-assembly and thermoresponsive properties.
- This technology offers potential for improved blood purification, reduced clinical costs, and enhanced patient outcomes.
- The surface exhibits excellent biocompatibility and resistance to non-specific protein adsorption.
