Literature DB >> 30096280

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

Benjamin R Clarkson1, Ernesto Freire2.   

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.
Copyright © 2018 Elsevier Inc. All rights reserved.

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

Mesh:

Substances:

Year:  2018        PMID: 30096280     DOI: 10.1016/j.ab.2018.08.006

Source DB:  PubMed          Journal:  Anal Biochem        ISSN: 0003-2697            Impact factor:   3.365


  2 in total

1.  Saliva profiling with differential scanning calorimetry: A feasibility study with ex vivo samples.

Authors:  Lena Pultrone; Raphael Schmid; Tuomas Waltimo; Olivier Braissant; Monika Astasov-Frauenhoffer
Journal:  PLoS One       Date:  2022-06-10       Impact factor: 3.752

2.  Construction of Bio-Based Polyurethanes via Olefin Metathesis and Their Thermal Reversible Behavior.

Authors:  Zizhao Liu; Gaosheng Gu; Junwu Chen; Zhongyu Duan; Binyuan Liu
Journal:  Polymers (Basel)       Date:  2022-08-31       Impact factor: 4.967

  2 in total

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