n-dodecyl-β-d-maltoside inhibits aggregation of human interferon-β-1b and reduces its immunogenicity

Robert A. Rifkin, Edward T. Maggio, Sonny Dike, Douglas A. Kerr, Michael Levy

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

The development of neutralizing antibodies to the protein drug interferon-β is a significant impediment to its use in the treatment of multiple sclerosis. Neutralizing antibodies to interferon-β arise from aggregation of the peptide during manufacturing and storage. We tested the ability of dodecylmaltoside, a nontoxic alkylsaccharide surfactant, to reduce aggregation of interferon-β in vitro and to reduce its immunogenicity in vivo. Interferon-β, in solution with and without dodecylmaltoside, was periodically evaluated for aggregation by light scatter for 1 month. Interferon-β, with and without dodecylmaltoside, was given 3 days/week for 1 month to mice; the sera of these mice were analyzed for anti-interferon-β antibodies by ELISA. Dodecylmaltoside reduces the aggregation of interferon-β in vitro and its immunogenicity in vivo. Our positive findings warrant additional tests of dodecylmaltoside as a therapeutic adjuvant in rodent models of multiple sclerosis.

Original languageEnglish (US)
Pages (from-to)158-162
Number of pages5
JournalJournal of Neuroimmune Pharmacology
Volume6
Issue number1
DOIs
StatePublished - Mar 2011

Keywords

  • disaccharides/chemistry
  • excipients
  • interferon-beta
  • multiple sclerosis

ASJC Scopus subject areas

  • Neuroscience (miscellaneous)
  • Immunology and Allergy
  • Immunology
  • Pharmacology

Fingerprint

Dive into the research topics of 'n-dodecyl-β-d-maltoside inhibits aggregation of human interferon-β-1b and reduces its immunogenicity'. Together they form a unique fingerprint.

Cite this