The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
PASylation: a biological alternative to PEGylation for extending the plasma half-life of pharmaceutically active proteins
Open accessAbstract
A major limitation of biopharmaceutical proteins is their fast clearance from circulation via kidney filtration, which strongly hampers efficacy both in animal studies and in human therapy. We have developed conformationally disordered polypeptide chains with expanded hydrodynamic volume comprising the small residues Pro, Ala and Ser (PAS). PAS sequences are hydrophilic, uncharged biological polymers with biophysical properties very similar to poly-ethylene glycol (PEG), whose chemical conjugation to drugs is an established method for plasma half-life extension. In contrast, PAS polypeptides offer fusion to a therapeutic protein on the genetic level, permitting Escherichia coli production of fully active proteins and obviating in vitro coupling or modification steps. Furthermore, they are biodegradable, thus avoiding organ accumulation, while showing stability in serum and lacking toxicity or immunogenicity in mice. We demonstrate that PASylation bestows typical biologics, such as interferon, growth hormone or Fab fragments, with considerably prolonged circulation and boosts bioactivity in vivo.
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Cites
Poly(ethylene glycol) in Drug Delivery: Pros and Cons as Well as Potential Alternatives
Knop, K., Hoogenboom, R., Fischer, D., & Schubert, U. S. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200902672 · Cited by 3,533
FcRn: the neonatal Fc receptor comes of age
Roopenian, D. C., & Akilesh, S. (2007) · Nature Reviews Immunology · doi:10.1038/nri2155 · Cited by 2,346
PEGylation of therapeutic proteins
Jevševar, S., Kunstelj, M., & Porekar, V. G. (2010) · Biotechnology Journal · doi:10.1002/biot.200900218 · Cited by 681
Cited by
Affibody Molecules in Biotechnological and Medical Applications
Ståhl, S., Gräslund, T., Eriksson Karlström, A., Frejd, F. Y., Nygren, P.-Å., & Löfblom, J. (2017) · Trends in Biotechnology · doi:10.1016/j.tibtech.2017.04.007 · Cited by 382
Aggregation of Protein Therapeutics Enhances Their Immunogenicity: Causes and Mitigation Strategies
Lundahl, M. L. E., Fogli, S., Colavita, P. E., & Scanlan, E. M. (2021) · RSC Chemical Biology · doi:10.1039/d1cb00067e · Cited by 212
Protein–polymer conjugation — moving beyond PEGylation
Qi, Y., & Chilkoti, A. (2015) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2015.08.009 · Cited by 176
Hinrichs, A., Kessler, B., Kurome, M., Blutke, A., Kemter, E., Bernau, M., Scholz, A. M., Rathkolb, B., Renner, S., Bultmann, S., et al. (2018) · Molecular Metabolism · doi:10.1016/j.molmet.2018.03.006 · Cited by 96
Metadata
- Authors
- Schlapschy, M., Binder, U., Borger, C., Theobald, I., Wachinger, K., Kisling, S., Haller, D., & Skerra, A.
- Venue
- Protein Engineering Design and Selection
- Publisher
- Oxford University Press (OUP)
- Published
- 2013-06-10
- Volume
- 26
- Issue
- 8
- Pages
- 489-501
- ISSN
- 0269-2139 (ISSN-L)
- 1741-0126
- 1741-0134
- OpenAlex
- W2161892929
- Cited by
- 342
- References
- 3
- FWCI
- 9.01
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Schlapschy, M., Binder, U., Borger, C., Theobald, I., Wachinger, K., Kisling, S., Haller, D., & Skerra, A. (2013). PASylation: a biological alternative to PEGylation for extending the plasma half-life of pharmaceutically active proteins. Protein Engineering Design and Selection. https://doi.org/10.1093/protein/gzt023
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