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Preparation and Characterization of SDF-1α-Chitosan-Dextran Sulfate Nanoparticles
Published on: January 22, 2015
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A zwitterionic serine modified chitosan derivative for improving protein stability and activity
Ye He1, Xingxian Wu1, Guanglin Zhang1
1Department of Materials Science and Engineering, College of Chemistry and Materials, Jinan University, Guangzhou 510632, PR China.
International Journal of Biological Macromolecules
|September 17, 2020
Summary
Zwitterionic phosphoryldiserine (PDS)-chitosan conjugates were synthesized and characterized. These PDS-chitosan materials exhibit excellent cell compatibility and effectively maintain protein structure and function in biomedical applications.
Area of Science:
- Biomaterials Science
- Polymer Chemistry
- Biochemistry
Background:
- Chitosan is a biocompatible polysaccharide with potential in biomedical applications.
- Modifying chitosan with zwitterionic groups can enhance its properties.
- Phosphoryldiserine (PDS) is a zwitterionic molecule that can be conjugated to polymers.
Purpose of the Study:
- To synthesize and characterize a zwitterionic phosphoryldiserine (PDS)-chitosan conjugate.
- To evaluate the cell compatibility and protein stabilization capabilities of the synthesized conjugate.
- To explore the potential of PDS-chitosan in maintaining protein function for biomedical uses.
Main Methods:
- Synthesis of PDS-chitosan conjugate via Atherton-Todd reaction.
- Characterization using NMR, ICP, FTIR, and XRD.
- In vitro cytotoxicity and hemolysis assays.
- UV-Vis adsorption and fluorescence spectroscopy to assess protein conformation and stability.
- Enzyme activity assays to evaluate protein function.
Main Results:
- Successful synthesis and structural characterization of PDS-chitosan conjugate.
- Confirmation of freezing bound water due to PDS incorporation, enhancing thermal properties.
- Excellent in vitro cell compatibility and low hemolysis.
- Demonstrated ability of PDS-chitosan to maintain native conformation and thermal stability of model protein bovine serum albumin (BSA).
- Enhanced esterase-like activity of BSA at low PDS-chitosan concentrations.
Conclusions:
- Zwitterionic PDS-chitosan conjugate exhibits superior biocompatibility and cell compatibility.
- PDS-chitosan effectively preserves protein native structure and enhances thermal stability.
- The conjugate shows potential for improving protein function, indicating significant promise for biomedical applications.

