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Screening of reducing agents for the PEGylation of recombinant human IL-10.
Ambrogelly, Alexandre; Cutler, Collette; Paporello, Brittany.
Afiliación
  • Ambrogelly A; Bioprocess Development, Merck Research Laboratories, Union, NJ 07083-7197, USA. alexandre.ambrogelly@merck.com
Protein J ; 32(5): 337-42, 2013 Jun.
Article en En | MEDLINE | ID: mdl-23657524
PEGylation is a technology commonly used to enhance the bioavailability of therapeutic proteins in patients. Reductive alkylation of a protein amino terminal alpha amine in the presence of a polyethylene glycol (PEG) chain derivatized with propionaldehyde and a reducing agent, typically sodium cyanoborohydride, is one of the technologies available to achieve quantitative and site specific PEGylation. While cyanoborohydride has proven to be a robust and efficient reagent for this type of reaction, it generates aqueous cyanide as a reaction by-product (and its corollary, the very volatile hydrogen cyanide). We report here the screening of reducing agents such as dimethylamine borane, trimethylamine borane, triethylamine borane, tert-butylamine borane, morpholine borane, pyridine borane, 2-picoline borane, and 5-ethyl-2-methyl-pyridine borane as alternatives to cyanoborohydride for the PEGylation of recombinant human IL-10. The results of our study show that pyridine borane and 2-picoline borane promote rhIL-10 PEGylation at levels comparable to those observed with cyanoborohydride.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Interleucina-10 / Sustancias Reductoras Tipo de estudio: Diagnostic_studies / Screening_studies Límite: Humans Idioma: En Revista: Protein J Asunto de la revista: BIOQUIMICA Año: 2013 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Interleucina-10 / Sustancias Reductoras Tipo de estudio: Diagnostic_studies / Screening_studies Límite: Humans Idioma: En Revista: Protein J Asunto de la revista: BIOQUIMICA Año: 2013 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos