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    Releasable Conjugation of Polymers to Proteins
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    † Swiss Federal Institute of Technology Zurich (ETHZ), Department of Chemistry and Applied Biosciences, Institute of Pharmaceutical Sciences, Vladimir-Prelog-Weg 1−5/10, 8093 Zurich, Switzerland
    ‡ Institut National de la Recherche Scientifique (INRS), EMT Research Centre, 1650 boul. Lionel-Boulet, Varennes, J3X 1S2, Canada
    *E-mail: [email protected]. Telephone: +1 514 228 69 32. Fax: +1 450 929 81 02.
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    Bioconjugate Chemistry

    Cite this: Bioconjugate Chem. 2015, 26, 7, 1172–1181
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    https://doi.org/10.1021/bc500611k
    Published January 22, 2015
    Copyright © 2015 American Chemical Society
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    Many synthetic strategies are available for preparing well-defined conjugates of peptides/proteins and polymers. Most reports on this topic involve coupling methoxy poly(ethylene glycol) to therapeutic proteins, a process referred to as PEGylation, to increase their circulation lifetime and reduce their immunogenicity. Unfortunately, the major dissuading dogma of PEGylation is that, in many cases, polymer modification leads to significant (or total) loss of activity/function. One approach that is gaining momentum to address this challenge is to release the native protein from the polymer with time in the body (releasable PEGylation). This contribution will present the state-of-the-art of this rapidly evolving field, with emphasis on the chemistry behind the release of the peptide/protein and the means for altering the rate of release in biological fluids. Linkers discussed include those based on the following: substituted maleic anhydride and succinates, disulfides, 1,6-benzyl-elimination, host–guest interactions, bicin, β-elimination, biodegradable polymers, E1cb elimination, β-alanine, photoimmolation, coordination chemistry, zymogen activation, proteolysis, and thioesters.

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    Bioconjugate Chemistry

    Cite this: Bioconjugate Chem. 2015, 26, 7, 1172–1181
    Click to copy citationCitation copied!
    https://doi.org/10.1021/bc500611k
    Published January 22, 2015
    Copyright © 2015 American Chemical Society
    Request reuse permissions

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