V. Skarda et F. Rypacek, PERMEATION OF PROTEINS THROUGH A BIODEGRADABLE HYDROGEL, Journal of bioactive and compatible polymers, 12(3), 1997, pp. 186-195
The permeation of proteins of different molecular weights into a biode
gradable hydrogel, a model system for controlled release of biological
ly active macromolecules, was investigated. The hydrogels were prepare
d by a crosslinking copolymerization from a biodegradable synthetic po
lypeptide, poly[N-5-(2-hydroxyethyl)-L-glutamine] (PHEG) with methacry
loylated side chains and acrylamide. The permeation of sodium azide, t
rypsin-kallikrein inhibitor (TKI), trypsin, and albumin into the gels
with network densities between 0.04 and 0.226 mmol/mL were determined.
The permeation of sodium azide was not influenced by the gel network
density. The permeability of TKI and trypsin was controlled by gels wi
th permeability coefficients ranging from 2.8 x 10(-9) to 4.0 x 10(-10
) mmol/mL. Gels with different network densities controlled the diffus
ion of peptides and proteins with molecular weights between 6,000 and
60,000. The combined effect of diffusion and biodegradation of the gel
on the permeation rate of macromolecules was determined for ly-alpha,
beta-[N-(2-hydroxyethyl)-DL-aspartamide]. A decrease in the gel cross-
linking density due to the degradation efficiently increased the perme
ability to the model macromolecule.