Enhanced Bioactivity of a Human GHR Antagonist Generated by Solid-Phase Site-Specific PEGylation.

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Title

Enhanced Bioactivity of a Human GHR Antagonist Generated by Solid-Phase Site-Specific PEGylation.

Content partner

The University of Auckland Library

Collection

ResearchSpace@Auckland

Description

Growth hormone (GH) has been implicated in cancer progression andis a potential target for anticancer therapy. Currently, pegvisomant is the only GH receptor (GHR) antagonist approved for clinical use. Pegvisomant is a mutated GH molecule (B2036) which is PEGylated on amine groups to extend serum half-life. However, PEGylation significantly reduces the bioactivity of the antagonist in mice. To improve bioactivity, we generated a series of B2036 conjugates with the site-specific attachment of ...

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Format

Research paper

Research format

Journal article

Date created

2021-02

Creator

Wang, Yue / Langley, Ries J / Tamshen, Kyle / Harms, Julia / Middleditch, Martin J / Maynard, Heather D / Jamieson, Stephen MF / Perry, Jo K

URL

https://hdl.handle.net/2292/64129

Related subjects

Animals / Humans / Mice / Escherichia coli / Cysteine / Growth Hormone / Recombinant Proteins / Dimerization / Science & Technology / Life Sciences & Biomedicine / Physical Sciences / Biochemistry & Molecular Biology / Chemistry, Organic / Polymer Science / Chemistry / HUMAN GROWTH-HORMONE / RECEPTOR ANTAGONISTS / EXTRACELLULAR DOMAIN / CRYSTAL-STRUCTURE / RATIONAL DESIGN / HALF-LIFE / ACTIVATION / PEGVISOMANT / MECHANISM / DIMERS / 03 Chemical Sciences / 06 Biological Sciences / 09 Engineering

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