Polyphenolic disaccharides endow proteins with unusual resistance to aggregation
Autor: | Anne Marie Hickey, Peter M. Tessier, Ali Reza A. Ladiwala, Jonathan S. Dordick, Joseph M. Perchiacca, Moumita Bhattacharya, Bonnie G. Domigan, Zachary S. Fishman |
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Rok vydání: | 2012 |
Předmět: |
Protein Folding
Hot Temperature Excipient Bioengineering Protein aggregation Disaccharides Applied Microbiology and Biotechnology Excipients chemistry.chemical_compound medicine Monosaccharide chemistry.chemical_classification Cyclodextrin Protein Stability Polyphenols Proteins food and beverages Glycoside Trehalose Aglycone Solubility chemistry Biochemistry Polyphenol Biotechnology medicine.drug |
Zdroj: | Biotechnology and Bioengineering. 109:1869-1874 |
ISSN: | 0006-3592 |
DOI: | 10.1002/bit.24460 |
Popis: | Protein aggregation is a common problem during the purification and formulation of therapeutic proteins. Here we report that polyphenolic disaccharides are unusually effective at preventing protein aggregation. We find that two polyphenolic glycosides-naringin and rutin-endow diverse proteins with the ability to unfold without aggregating when heated, as well as the ability to refold without aggregating when cooled at low glycoside concentrations ( |
Databáze: | OpenAIRE |
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