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 language | English (US) |
|---|---|
| Pages (from-to) | 50-52 |
| Number of pages | 3 |
| Journal | Analytical Biochemistry |
| Volume | 558 |
| DOIs | |
| State | Published - Oct 1 2018 |
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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 journal › Article
}
TY - JOUR
T1 - Isothermal calorimetry of a monoclonal antibody using a conventional differential scanning calorimeter
AU - Clarkson, Benjamin R.
AU - Freire, Ernesto I
PY - 2018/10/1
Y1 - 2018/10/1
N2 - 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.
AB - 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.
KW - Differential scanning calorimetry
KW - Isothermal calorimetry
KW - Protein denaturation
KW - Protein stability
UR - http://www.scopus.com/inward/record.url?scp=85051277541&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85051277541&partnerID=8YFLogxK
U2 - 10.1016/j.ab.2018.08.006
DO - 10.1016/j.ab.2018.08.006
M3 - Article
C2 - 30096280
AN - SCOPUS:85051277541
VL - 558
SP - 50
EP - 52
JO - Analytical Biochemistry
JF - Analytical Biochemistry
SN - 0003-2697
ER -