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

• 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
• ISSN: 1063-7850; 1090-6533
• DOI: 10.1134/S1063785017120045

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.