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

Benjamin R Clarkson; Ernesto Freire

doi:10.1016/j.ab.2018.08.006

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

Anal Biochem. 2018 Oct 1:558:50-52. doi: 10.1016/j.ab.2018.08.006. Epub 2018 Aug 7.

Authors

Benjamin R Clarkson¹, Ernesto Freire²

Affiliations

¹ Department of Biology, Johns Hopkins University, 3400 North Charles, Baltimore, MD, 21218, United States.
² Department of Biology, Johns Hopkins University, 3400 North Charles, Baltimore, MD, 21218, United States. Electronic address: ef@jhu.edu.

PMID: 30096280
DOI: 10.1016/j.ab.2018.08.006

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 T_m. 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 T_m. 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.

Keywords: Differential scanning calorimetry; Isothermal calorimetry; Protein denaturation; Protein stability.

Publication types

Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Antibodies, Monoclonal / analysis*
Antibodies, Monoclonal / chemistry
Calorimetry / methods
Calorimetry, Differential Scanning / instrumentation*
Calorimetry, Differential Scanning / methods*
Kinetics
Protein Denaturation
Temperature

Substances

Antibodies, Monoclonal