ArticleNature communications2024
Exactly defined molecular weight poly(ethylene glycol) allows for facile identification of PEGylation sites on proteins.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed.
- Dynamic modulation of immune-neural axis via controlled magnesium-releasing nanocapsules accelerates cranial bone regeneration.Journal of nanobiotechnology · 2026Article
- Cysteine Pegylation of a Mutant L-asparaginase Affords Enhanced Activity and Thermostability. A Comparative Study Against N-terminal Conjugation.Applied biochemistry and biotechnology · 2026Article
- Raman Spectroscopic Classification of Polyethylene Glycol Samples of Varying Molecular Weights Using Machine Learning.Molecules (Basel, Switzerland) · 2026Article
- Site-specific PEGylation of proteins: Insights into structural and functional changes.Acta pharmaceutica Sinica. B · 2025Review
- Biomolecule-functionalized dental implant surfaces: Towards augmenting soft tissue integration.Bioactive materials · 2025Review
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PEGylation (the covalent attachment of one or more poly(ethylene glycol) (PEG) units to a therapeutic) is a well-established technique in the pharmaceutical industry to increase blood-residence time and decrease immunogenicity. A challenging aspect of PEGylation is the dispersity of PEGylation agents, which results in batch-to-batch variations and analytical limitations. Herein, we present an approach to overcome these limitations by manufacturing a defined molecular weight (dispersity-free) PEGylation agent. We synthesise a defined molecular weight (M
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Registered trials
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