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Biomedical subjects

J M Bezemer

Publications and source records attributed to J M Bezemer.

20 records · Page 2Linked to original sources

A controlled release system for proteins based on poly(ether ester) block-copolymers: polymer network characterization.

The properties of a series of multiblock copolymers, based on hydrophilic poly(ethylene glycol) (PEG) and hydrophobic poly(butylene terephthalate) (PBT) blocks were investigated with respect to their application as a matrix for controlled release of proteins. The degree of swelling, Q, of the copolymers increased with increasing PEG content and with increasing molecular weight of the PEG segment. Within the composition range tested, Q varied from 1.26 for polymers with PEG segments of 600 g/mol and a PBT content of 60 weight.% up to 3.64 for polymers with PEG segments of 4000 g/mol and a PEG/PBT weight ratio of 80:20. Equilibrium stress (compression)-strain measurements were performed in order to estimate mesh sizes. The mesh size of the copolymers ranged from 38 to 93 A, which was experimentally confirmed by diffusion of vitamin B(12) (hydrodynamic diameter d(h)=16.6 A), lysozyme (d(h)=41 A) and bovine serum albumin (d(h)=72 A). The in vitro degradation of PEG/PBT copolymers with a PEG block length of 1000 g/mol and PEG/PBT weight ratios of 70:30, 60:40 and 40:60 was studied. Matrices with increasing PEG contents exhibited a faster weight loss in phosphate-buffered saline (pH 7.4) at 37 degrees C. Over a degradation period of 54 days, M(n) decreased by about 35-45%, while the composition of the matrices, determined by NMR, remained almost constant.

Animals↗

Poly(ethylene oxide)-modified carboxylated polystyrene latices--immobilization chemistry and protein adsorption.

alpha,omega-Diamino poly(ethylene oxides) (PEOs) with different molecular weights (148, 1000, and 3400) were covalently immobilized onto carboxylated polystyrene latices. The immobilization of PEO was carried out with N-(3-dimethylaminopropyl)-N'-ethylcarbodiimide (EDC) and N-hydroxysuccinimide (NHS) in aqueous media. The reaction conditions were optimized to obtain a maximal coupling of PEO. The degree of coupling was determined by the surface concentration of amino groups. The maximal surface concentrations of amino groups were close to what is expected for a complete coverage of the surface with PEO. Adsorption of albumin from a buffer solution onto PEO-containing surfaces was about 85% less than the albumin uptake by unmodified polystyrene latices. Protein adsorption from plasma dilutions was lower on surfaces containing PEO molecules with a higher molecular weight. The reduction of the protein uptake from plasma by surfaces containing PEO-3400 molecules was only 40% compared to the adsorption to unmodified surfaces. These results indicate that plasma proteins have a low affinity for surfaces modified with PEO. However the PEO modified surfaces are by no means 'protein resistant' when exposed to plasma.

Adsorption↗