Freeze/thaw of IGG solutions

Jacqueline Horn, Sampeeti Jena, Alptekin Aksan, Wolfgang Friess

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

In this communication, the effect of mannitol and trehalose crystallization on the unfolding of IgG 1 , a monoclonal antibody, in the frozen state with repeat freeze/thaw under different pH conditions was explored. Formulations were annealed at −20 °C for 20 h five times (interrupted by freeze/thaw). This was done to induce excipient crystallization. Characterization of the frozen-thawed samples was performed by circular dichroism, particle analysis, and size exclusion chromatography. At a pH of 3, formation of insoluble and soluble aggregates was observed however, these could be reduced by the use of a surfactant. Cryoprotectant free formulations showed higher monomer content after freeze/thaw. At pH 5, a single freeze/thaw cycle did not result in a significant increase in particle numbers. At pH range of 4–7 however, aggregate formation in the size range of 1–25 µm was observed after 5 freeze/thaw cycles.

Original languageEnglish (US)
Pages (from-to)185-189
Number of pages5
JournalEuropean Journal of Pharmaceutics and Biopharmaceutics
Volume134
DOIs
StatePublished - Jan 2019

Bibliographical note

Funding Information:
This work was partially funded by an NSF grant ( CBET-1335936 ) to AA.

Funding Information:
This work was partially funded by an NSF grant (CBET-1335936) to AA.

Publisher Copyright:
© 2018 Elsevier B.V.

Copyright:
Copyright 2019 Elsevier B.V., All rights reserved.

Keywords

  • Crystallization
  • Freeze/thaw
  • Monoclonal antibody
  • Stability
  • pH

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