Controlled release of polypeptides from polyanhydrides

Ron E, E Ron, Turek T, T Turek, E Mathiowitz, Mathiowitz E, M Chasin, Chasin M, M Hageman, Hageman M, R Langer, Langer R
Proceedings of the National Academy of Sciences of the United States of America · 1993 · vol. 90(9) , pp. 4176–80 · doi:10.1073/pnas.90.9.4176 · PMID:8483931 · PMC46469
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Researchers investigated how polymer hydrophobicity and stabilizers affect protein release, finding that highly hydrophobic polyanhydrides with sucrose enabled the intact release of recombinant bovine somatotropin and zinc insulin over three weeks.

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Abstract

The effects of both polymer hydrophobicity and addition of stabilizers on the release and integrity of polymer-encapsulated proteins were studied. By using very hydrophobic poly[1,3-bis(p-carboxyhydroxy)hexane anhydride] with sucrose as an excipient, both recombinant bovine somatotropin and zinc insulin were released intact over 3 weeks. The released proteins appeared to maintain their integrity as judged by acidic reverse-phase HPLC, size-exclusion HPLC, radioimmunoassay, and conformation-sensitive immunoassays. Our results also suggest how polymer hydrophobicity can be used to enhance protein stability.

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MeSH descriptors

Decanoic Acids Growth Hormone Insulin Polyesters Animals Cattle Delayed-Action Preparations Drug Carriers Immunoassay Indicators and Reagents Kinetics Recombinant Proteins Spectrophotometry, Infrared Time Factors

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