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Effect of polymer chemistry and fabrication method on protein release and stability from polyanhydride microspheres
Author(s) -
Lopac Senja K.,
Torres Maria P.,
WilsonWelder Jennifer H.,
Wannemuehler Michael J.,
Narasimhan Balaji
Publication year - 2009
Publication title -
journal of biomedical materials research part b: applied biomaterials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.665
H-Index - 108
eISSN - 1552-4981
pISSN - 1552-4973
DOI - 10.1002/jbm.b.31478
Subject(s) - ovalbumin , chemistry , polymer , monomer , kinetics , sebacic acid , emulsion , miniemulsion , aqueous solution , polymer chemistry , chemical engineering , nuclear chemistry , organic chemistry , antigen , genetics , physics , quantum mechanics , engineering , biology
The release kinetics and stability of ovalbumin encapsulated into polyanhydride microspheres with varying chemistries were studied. Polymers based on the anhydride monomers sebacic acid (SA), 1,6‐bis( p ‐carboxyphenoxy)hexane (CPH), and 1,8‐bis ( p ‐carboxyphenoxy)‐3,6‐dioxaoctane (CPTEG) were utilized. Microspheres were fabricated using two non‐aqueous methods: a solid/oil/oil double emulsion technique and cryogenic atomization. The studies showed that the two fabrication methods did not significantly affect the release kinetics of ovalbumin, even though the burst release of the protein was a function of the fabrication method and the polymer chemistry. Antigenic stability of ovalbumin released from microspheres prepared by cryogenic atomization was studied by western blot analysis. These studies indicate that the amphiphilic CPTEG:CPH polyanhydrides preserved protein structure and enhanced protein stability by preserving the immunological epitopes of released protein. © 2009 Wiley Periodicals, Inc. J Biomed Mater Res Part B: Appl Biomater, 2009