Premium
Photopolymerizable Hydrogels Made from Polymer‐Conjugated Albumin for Affinity‐Based Drug Delivery
Author(s) -
OssRonen Liat,
Seliktar Dror
Publication year - 2010
Publication title -
advanced engineering materials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.938
H-Index - 114
eISSN - 1527-2648
pISSN - 1438-1656
DOI - 10.1002/adem.200980005
Subject(s) - pegylation , albumin , self healing hydrogels , drug delivery , peg ratio , naproxen , materials science , ethylene glycol , serum albumin , drug carrier , chemistry , conjugated system , polyethylene glycol , biophysics , chromatography , polymer , polymer chemistry , organic chemistry , biochemistry , medicine , biology , alternative medicine , finance , pathology , economics
As a drug delivery vehicle, biodegradable albumin hydrogels can combine the high binding capacity of albumin with the structural stability of a polymeric hydrogel network to enable controlled release of small molecules based on both binding affinity and physical interactions. In the present study, we report on the development of a hybrid hydrogel composed of albumin conjugated to poly(ethylene glycol) (PEG) for drug delivery applications where controlled release is accomplished using the natural affinity of the drugs to the serum albumin. Bovine serum albumin was conjugated to PEG‐diacrylate having a molecular weight of 1.5, 4, or 10 kDa to form a PEGylated albumin macromolecule (mono‐PEGylated or multi‐PEGylated). Biodegradable hydrogels were formed from the PEGylated albumin using photopolymerization. Two model drugs, Warfarin and Naproxen, were used for equilibrium dialysis and release experiments from the hydrogels, both having relatively low molecular weights and a known high affinity for albumin. Equilibrium dialysis experiments showed that multi‐PEGylation of albumin significantly decreased the drug affinity to the protein compared to non‐PEGylated controls, irrespective of the PEG molecular weight. However, the results from drug release experiments showed that mono‐PEGylation of albumin did not change its natural affinity to the drug. Comparing the release profiles with a Fickian diffusion model provided strong evidence that hydrogels containing mono‐PEGylated albumin exhibited sub‐diffusive drug release properties based on the affinity of the drug to the tethered protein.