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The Conformation of Poly(ethylene glycol) Chains in Mono-PEGylated Lysozyme and Mono-PEGylated Human Growth Hormone

Published

Author(s)

Sheetal S. Pai, Boualem Hammouda, Kunlun Hong, Danilo.C. Pozzo, Todd M. Przybycien, Robert D. Tilton

Abstract

Covalent conjugation of poly(ethylene glycol) or "PEGylation" has proven an effective strategy to improvement pharmaceutical protein efficacy. Understanding the configuration of conjugated PEG chains is necessary to interpret the effect of PEG conjugation on renal clearance rates and steric protection of circulation proteins in vivo. Mono-PEGylated proteins are typically described as having a protective PEG shroud wrapped around the protein, but recent dynamic light scattering studies have suggested that conjugates adopt a dumbbell configuration, with a relatively unperturbed PEG random coil adjacent to the globular protein. We used Small-Angle Neutron Scattering (SANS) to distinguish between the dumbbell model and the shroud model for chicken egg lysozyme and human growth hormone covalently conjugated to a single 20 kDa PEG chain. the SANS contrast variation technique was used to isolate the PEG portion of the conjugate. Scattering intensity profiles were well described by the dumbbell model and inconsistent with the shroud model.
Citation
Bioconjugate Chemistry
Volume
22

Keywords

lysozyme, human growth hormone, poly(ethylene glycol), small-angle neutron scattering, SANS

Citation

Pai, S. , Hammouda, B. , Hong, K. , Pozzo, D. , Przybycien, T. and Tilton, R. (2011), The Conformation of Poly(ethylene glycol) Chains in Mono-PEGylated Lysozyme and Mono-PEGylated Human Growth Hormone, Bioconjugate Chemistry, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=908569 (Accessed April 18, 2024)
Created September 27, 2011, Updated October 12, 2021