Effects of compaction and storage conditions on stability of intravenous immunoglobulin – Implication on developing oral tablets of biologics

Yuwei Lu, Chenguang Wang, Bowen Jiang, Changquan Calvin Sun, Stephen W. Hoag

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


Biological products, such as therapeutic proteins, vaccines and cell - based therapeutics have a rapidly growing global market. Monoclonal antibody represents a major portion of the biologics market. For biologics that target gastrointestinal tract, the oral delivery route offers many advantages, such as better patient compliance, easy administration and increased stability, over the parental route of administration. To lay the ground work for the oral delivery of biologics, we studied the solid state properties and effects of compaction pressure, particle size, and storage relative humidity on the stability of immunoglobulin G (IVIG). We employed complementary analytical and biophysical techniques, such as size exclusion chromatography and Dynamic light scattering to characterize the aggregates, circular dichroism and solid state Fourier-transform infrared spectroscopy to evaluate protein secondary structure and nano-DSC to probe thermal stability of protein conformations. Our results showed storage relative humidity could induce conformational changes and aggregation of IVIG. However, the IVIG binding activity did not significantly change with relative humidity. The commonly used compaction pressures did not promote protein aggregation, but noticeably reduced binding activity.

Original languageEnglish (US)
Article number120737
JournalInternational journal of pharmaceutics
StatePublished - Jul 15 2021

Bibliographical note

Funding Information:
The authors thank Dr. Robert Brinson and Dr. Amanda Alterie from University of Maryland – Institute for Bioscience and Biotechnology Research on the training and technical supports for Nano- DSC and CD. Parts of this work were carried out in the Characterization Facility, University of Minnesota, a member of the NSF-funded Materials Research Facilities Network (www.mrfn.org) via the MRSEC program. This manuscript is in partial fulfillment of the requirements for the degree of Doctor of Philosophy for Yuwei Lu at University of Maryland Baltimore.

Publisher Copyright:
© 2021 Elsevier B.V.


  • Aggregation
  • Immunoglobulin
  • Mechanical properties
  • Monoclonal antibody
  • Oral tablet

PubMed: MeSH publication types

  • Journal Article


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