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Encapsulation and delivery of protein from within poly(sulfobetaine) hydrogel beads
Author(s) -
Erfani Amir,
Flynn Nicholas H.,
Aichele Clint P.,
Ramsey Joshua D.
Publication year - 2020
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.49550
Subject(s) - self healing hydrogels , bovine serum albumin , monomer , methacrylate , swelling , polymer chemistry , chemistry , radical polymerization , chemical engineering , thermal stability , lower critical solution temperature , polymerization , polymer , biophysics , materials science , copolymer , chromatography , organic chemistry , engineering , biology
Advancement of therapeutic protein therapies can be hindered by their poor stability and short in vivo half‐life. There is emerging evidence that biocompatible zwitterionic materials can prevent nonspecific interactions within proteins systems that contribute to protein instability. Here, zwitterionic hydrogel beads are synthesized from poly(sulfobetaine methyl methacrylate), pSB, using an inverse emulsion, free radical polymerization reaction technique. The transport properties within the zwitterionic hydrogels were characterized using 1 H NMR diffusometry. Equilibrium water content as high as 0.90 was measured for the synthesized hydrogels. Our study revealed that the pSB hydrogels are nontoxic, ion responsive, and their swelling is temperature dependent. The zwitterionic hydrogel beads were capable of undergoing lyophilization without aggregation. Hydrogel beads were loaded with a model protein, bovine serum albumin (BSA), using a postfabrication loading technique. The protein loading was studied using confocal laser microscopy, indicating homogenous protein dispersion of up to 40 μg BSA/mg hydrogel within the beads. Furthermore, the release rate of the protein from the synthesized hydrogel was studied at different crosslinker to monomer ratios. The protein encapsulated within the zwitterionic hydrogel had slower rates of thermal aggregation compared to nonencapsulated protein in solution. Furthermore, the protein‐loaded inside the zwitterionic hydrogel better maintained its bioactivity.