The DOI matches its Crossref record; 180 of the 180 references it cites were found in a registry or an index.
Glycosylation of Therapeutic Proteins: An Effective Strategy to Optimize Efficacy
Open accessAbstract
During their development and administration, protein-based drugs routinely display suboptimal therapeutic efficacies due to their poor physicochemical and pharmacological properties. These innate liabilities have driven the development of molecular strategies to improve the therapeutic behavior of protein drugs. Among the currently developed approaches, glycoengineering is one of the most promising, because it has been shown to simultaneously afford improvements in most of the parameters necessary for optimization of in vivo efficacy while allowing for targeting to the desired site of action. These include increased in vitro and in vivo molecular stability (due to reduced oxidation, cross-linking, pH-, chemical-, heating-, and freezing-induced unfolding/denaturation, precipitation, kinetic inactivation, and aggregation), as well as modulated pharmacodynamic responses (due to altered potencies from diminished in vitro enzymatic activities and altered receptor binding affinities) and improved pharmacokinetic profiles (due to altered absorption and distribution behaviors, longer circulation lifetimes, and decreased clearance rates). This article provides an account of the effects that glycosylation has on the therapeutic efficacy of protein drugs and describes the current understanding of the mechanisms by which glycosylation leads to such effects.
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Cites
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Cited by
Strategies for extended serum half-life of protein therapeutics
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Engineering protein-based therapeutics through structural and chemical design
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Glycosylation of extracellular vesicles: current knowledge, tools and clinical perspectives
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Metadata
- Authors
- Solá, R. J., & Griebenow, K.
- Venue
- BioDrugs
- Published
- 2010-02
- Volume
- 24
- Issue
- 1
- Pages
- 9-21
- ISSN
- 1172-7039 (ISSN-L)
- 1173-8804
- OpenAlex
- W2027894892
- Cited by
- 440
- References
- 180
- FWCI
- 8.51
- Type
- journal article
- Language
- en
- Open access
- green
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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