6533b7dbfe1ef96bd1270b20

RESEARCH PRODUCT

CONTROLLED RELEASE OF IgG BY NOVEL UV INDUCED POLYSACCHARIDE/POLY(AMINO ACID)HYDROGELS

Giovanna PitarresiGaetano GiammonaFabio Salvatore PalumboGennara CavallaroGiuseppe Tripodo

subject

Polymers and PlasticsUltraviolet RaysMethacrylic anhydrideBioengineeringPeptideContext (language use)Enzyme-Linked Immunosorbent AssayBiomaterialschemistry.chemical_compoundCrohn DiseasePolysaccharidesMaterials ChemistryOrganic chemistryHumanshydrogels drug releaseAmino Acidschemistry.chemical_classificationChromatographytechnology industry and agricultureSuccinic anhydrideHydrogelsControlled releaseAmino acidchemistrySettore CHIM/09 - Farmaceutico Tecnologico ApplicativoDelayed-Action PreparationsImmunoglobulin GSelf-healing hydrogelsChromatography GelCaco-2 CellsDrug carrierBiotechnology

description

The development of new protein and peptide drugs needs new delivery systems able to entrap such drugs in safe conditions without affecting their structure and biological activity. In this context, the present work reports a new approach to load IgG, used as a model of therapeutic proteins such as anti-TNF-alpha monoclonal antibodies, into a polymeric system able to release the entrapped IgG in a controlled manner. In particular, new polysaccharide/poly(amino acid) UV induced hydrogels are proposed as colon delivery systems for human IgG. The poly(amino acid), alpha,beta-poly[N-(2-hydroxyethyl)-D,L-aspartamide], has been functionalized with methacrylic anhydride, while the polysaccharide, inulin, has been functionalized with methacrylic anhydride and succinic anhydride. The hydrogels were obtained by a short-time UV irradiation, in physiological-like conditions, without the use of radical initiators, at low temperature and in the presence or in the absence of PEGDM(550) used as a co-crosslinker in order to evaluate potential differences in terms of physicochemical properties and release profile. The obtained hydrogels were degradable by inulinase, showed a high cell compatibility and the released antibodies, analyzed by SEC and ELISA, retained their biological activity.

10.1002/mabi.200800181http://hdl.handle.net/10447/39502