Isothermal calorimetry of a monoclonal antibody using a conventional differential scanning calorimeter

Benjamin R. Clarkson, Ernesto I Freire

Research output: Contribution to journalArticle

Abstract

It has been shown that isothermal calorimetry is able to provide critical information regarding the kinetics of denaturation/aggregation of monoclonal antibodies at temperatures below Tm. Those measurements, however, required sophisticated specialized instrumentation. Here, we demonstrate that similar measurements can be performed using widely available conventional differential scanning calorimeters (DSC) when operated in isothermal scan mode. The denaturation/aggregation kinetics of the anti-HIV monoclonal antibody VRC07-523LS was measured by isothermal DSC at ten degrees below Tm. It is shown that a readily available instrument provides similar kinetic information and can become an important tool for determining the long term stability of biologics.

Original languageEnglish (US)
Pages (from-to)50-52
Number of pages3
JournalAnalytical Biochemistry
Volume558
DOIs
StatePublished - Oct 1 2018

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Calorimetry
Calorimeters
Denaturation
Monoclonal Antibodies
Scanning
Kinetics
Agglomeration
HIV Antibodies
Biological Products
Temperature

Keywords

  • Differential scanning calorimetry
  • Isothermal calorimetry
  • Protein denaturation
  • Protein stability

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Isothermal calorimetry of a monoclonal antibody using a conventional differential scanning calorimeter. / Clarkson, Benjamin R.; Freire, Ernesto I.

In: Analytical Biochemistry, Vol. 558, 01.10.2018, p. 50-52.

Research output: Contribution to journalArticle

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