Long-Acting Human Growth Hormone Receptor Antagonists Produced in E. coli and Conjugated with Polyethylene Glycol.

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Title

Long-Acting Human Growth Hormone Receptor Antagonists Produced in E. coli and Conjugated with Polyethylene Glycol.

Content partner

The University of Auckland Library

Collection

ResearchSpace@Auckland

Description

Growth hormone (GH) is a peptide hormone that mediates actions through binding to a cell surface GH receptor (GHR). The GHR antagonist, B2036, combines an amino acid substitution at 120 that confers GHR antagonist activity, with eight additional amino acid substitutions. Conjugation to polyethylene glycol (PEG) increases the serum half-life of these proteins due to reduced renal clearance. Recombinant forms of GH and its antagonists are mainly produced in prokaryotic expression systems, such ...

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Format

Research paper

Research format

Journal article

Date created

2020-06

Creator

Wang, Yue / Langley, Ries J / Tamshen, Kyle / Jamieson, Stephen M / Lu, Man / Maynard, Heather D / Perry, Jo K

URL

https://hdl.handle.net/2292/64130

Related subjects

Humans / Escherichia coli / Polyethylene Glycols / Human Growth Hormone / Amino Acid Substitution / Signal Transduction / Cell Proliferation / Dose-Response Relationship, Drug / Solubility / Half-Life / Biotechnology / 5 Development of treatments and therapeutic interventions / 5.1 Pharmaceuticals / Science & Technology / Life Sciences & Biomedicine / Physical Sciences / Biochemical Research Methods / Biochemistry & Molecular Biology / Chemistry, Multidisciplinary / Chemistry, Organic / Chemistry / SITE-SPECIFIC PEGYLATION / IN-VIVO / EXTRACELLULAR DOMAIN / RATIONAL DESIGN / FORM / PEGVISOMANT / PURIFICATION / EXPRESSION / CLEARANCE / PROLACTIN / 1103 Clinical Sciences / Biomedical / Basic Science / 1.1 Normal biological development and functioning / 0304 Medicinal and Biomolecular Chemistry / 0305 Organic Chemistry / 0601 Biochemistry and Cell Biology

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