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- W2050349885 endingPage "622" @default.
- W2050349885 startingPage "609" @default.
- W2050349885 abstract "With the advent of antibody fragments and alternative binding scaffolds, that are devoid of Fc-regions, strategies to increase the half-life of small proteins are becoming increasingly important. Currently, the established method is chemical PEGylation, but more elaborate approaches are being described such as polysialylation, amino acid polymers and albumin-binding derivatives. This article reviews the main strategies for pharmacokinetic enhancement, primarily chemical conjugates and recombinant fusions that increase apparent molecular weight or hydrodynamic radius or interact with serum albumin which itself has a long plasma half-life. We highlight the key chemical linkage methods that preserve antibody function and retain stability and look forward to the next generation of technologies which promise to make better quality pharmaceuticals with lower side effects. Although restricted to antibodies, all of the approaches covered can be applied to other biotherapeutics." @default.
- W2050349885 created "2016-06-24" @default.
- W2050349885 creator A5014973629 @default.
- W2050349885 creator A5045416930 @default.
- W2050349885 creator A5056862237 @default.
- W2050349885 date "2010-02-04" @default.
- W2050349885 modified "2023-10-15" @default.
- W2050349885 title "Modulating the pharmacokinetics of therapeutic antibodies" @default.
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- W2050349885 doi "https://doi.org/10.1007/s10529-010-0214-z" @default.
- W2050349885 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20131077" @default.
- W2050349885 hasPublicationYear "2010" @default.
- W2050349885 type Work @default.