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ABSTRACT: Background
Polyethylene glycol (PEG) is widely used in industry and medicine. Anti-PEG antibodies have been developed for characterizing PEGylated drugs and other applications. However, the underlying mechanism for specific PEG binding has not been elucidated.Methods
The Fab of two cognate anti-PEG antibodies 3.3 and 2B5 were each crystallized in complex with PEG, and their structures were determined by X-ray diffraction. The PEG-Fab interactions in these two crystals were analyzed and compared with those in a PEG-containing crystal of an unrelated anti-hemagglutinin 32D6-Fab. The PEG-binding stoichiometry was examined by using analytical ultracentrifuge (AUC).Results
A common PEG-binding mode to 3.3 and 2B5 is seen with an S-shaped core PEG fragment bound to two dy
SUBMITTER: Lee CC
PROVIDER: S-EPMC6945545 | biostudies-literature | 2020 Jan
REPOSITORIES: biostudies-literature