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Protein stability in controlled-release systems

Nature Biotechnology volume 18, pages 24–25 (2000)Cite this article

The ability to entrap drugs within, and subsequently release them from, polymers or liposomes has led to new treatments for a number of diseases. Despite major advances, however, the majority of these delivery systems are still used for small molecules taken orally, transdermally, parenterally, or through the nose or lung.1 The development of controlled-release systems for proteins involves additional challenges. The biggest single issue with formulations intended for long-term controlled release (days to months) is the instability of the proteins themselves. In this issue of Nature Biotechnology, Schwendeman and colleagues provide a new example of a rational approach to overcome protein degradation in a controlled-release system2.

In the 1970s, the conventional wisdom was that only small lipophilic molecules could be slowly delivered through polymeric vehicles3 and that large molecules, such as peptides and proteins, would be released either very rapidly or not at all. However, it was learned that by using the appropriate types of polymers and formulation techniques, molecules of any size and charge could be continuously released for over 100 days4, and by the end of the following decade, the first controlled-release system for a peptide had been approved by the FDA3.

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Authors and Affiliations

  1. K. Fu is a doctoral candidate, A.M. Klibanov is professor of chemistry, and R. Langer is Germeshausen professor of chemical and biomedical engineering at the Massachusetts Institute of Technology, Cambridge, MA

    K. Fu, A.M. Klibanov & R. Langer

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  1. K. Fu
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  2. A.M. Klibanov
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  3. R. Langer
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Fu, K., Klibanov, A. & Langer, R. Protein stability in controlled-release systems. Nat Biotechnol 18, 24–25 (2000). https://doi.org/10.1038/71875

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