Thermodynamic Analysis of the Conformational Stability of a Single-Domain Therapeutic Antibody

The stability of a new single-domain therapeutic antibody to the ErbB3 receptor was studied by fluorescence spectroscopy at different concentrations of a denaturing agent and temperatures. The analysis of experimental denaturation curves allowed us to build a complete thermodynamic model of unfoldin...

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Bibliographic Details
Published in:Technical physics letters 2017-12, Vol.43 (12), p.1088-1091
Main Authors: Eliseev, I. E., Yudenko, A. N., Besedina, N. A., Ulitin, A. B., Ekimova, V. M., Evdokimov, S. R., Putintceva, J. V., Yakovlev, P. A., Lomovskaya, M. I., Terterov, I. N., Bogdanov, A. A., Dubina, M. V.
Format: Article
Language:English
Subjects:
60 APPLIED LIFE SCIENCES
ANTIBODIES
BIOPHYSICS
Classical and Continuum Physics
CLASSICAL AND QUANTUM MECHANICS, GENERAL PHYSICS
CONCENTRATION RATIO
Denaturation
Fluorescence
FLUORESCENCE SPECTROSCOPY
Physics
Physics and Astronomy
RECEPTORS
STABILITY
Stability analysis
THERMODYNAMIC MODEL
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Summary:The stability of a new single-domain therapeutic antibody to the ErbB3 receptor was studied by fluorescence spectroscopy at different concentrations of a denaturing agent and temperatures. The analysis of experimental denaturation curves allowed us to build a complete thermodynamic model of unfolding and to determine all parameters of the transition: Δ G = 8.5 kcal mol –1 , T m = 76°C, Δ H m = 107 kcal mol –1 , Δ C p = 1.8 kcal K –1 mol –1 . The obtained data evidence the high stability of the antibody in a broad range of conditions, which is essential for further structural and functional studies and possible therapeutic application.
ISSN:1063-7850
1090-6533
DOI:10.1134/S1063785017120045