Lysozyme loading and release from hydrogels carrying pendant phosphate groups

-To develop a polymeric matrix for efficiently loading cationic biomolecules, polyelectrolyte hydrogels carrying pendant phosphate groups were synthesized by copolymerizing 2-methacryloyloxyethyl dihydrogen phosphate with N-isopropylacrylamide and N,N'-methylene-bis-acrylamide. The phosphate-ca...

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Bibliographic Details
Published in:Journal of biomaterials science. Polymer ed. 1998, Vol.9 (1), p.43-53
Main Authors: Nakamae, Katsuhiko, Nizuka, Takeshi, Miyata, Takashi, Furukawa, Manabu, Nishino, Takashi, Kato, Koichi, Inoue, Tadaaki, Hoffman, Allan S., Kanzaki, Yoshio
Format: Article
Language:English
Subjects:
Biocompatible Materials
Enzymes, Immobilized - metabolism
hydrogel
Hydrogel, Polyethylene Glycol Dimethacrylate
Hydrogen-Ion Concentration
Indicators and Reagents
Kinetics
lysozyme
Muramidase - metabolism
Osmolar Concentration
Phosmer M
Phosphates - chemical synthesis
polyelectrolyte
Polyethylene Glycols
polyion complex
Polymethacrylic Acids - chemical synthesis
Protein Binding
protein drug delivery
Protein loading
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Summary:-To develop a polymeric matrix for efficiently loading cationic biomolecules, polyelectrolyte hydrogels carrying pendant phosphate groups were synthesized by copolymerizing 2-methacryloyloxyethyl dihydrogen phosphate with N-isopropylacrylamide and N,N'-methylene-bis-acrylamide. The phosphate-carrying monomer yielded anionic hydrogels, which formed ionic complexes with the cationic protein, lysozyme. It was shown that the amount of complexed lysozyme reached 2.1 gg -1 dry gel, corresponding to 1.3 x 10 -3 mol phosphate group per gram lysozyme, when 40 mol% of phosphate-carrying monomer was incorporated in a hydrogel. When the hydrogel complexed with lysozyme was placed in deionized water and various KCl solutions, of varying concentrations of up to 0.5 M KCl, no lysozyme was released in deionized water, while increasing amounts of lysozyme were released as the KCl concentration increased. This confirmed that lysozyme was loaded in the hydrogel through electrostatic interactions. It was further found that the complexed lysozyme retained its enzymatic activity after being released from the hydrogel. These results suggest the use of this system for the controlled release of cationic protein drugs.
ISSN:0920-5063
1568-5624
DOI:10.1163/156856297X00254