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 Vol. 43; no. 12; pp. 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:	Journal Article
Language:	English
Published:	Moscow Pleiades Publishing 01-12-2017 Springer Nature B.V
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