Technical Physics Letters

, Volume 43, Issue 12, pp 1088–1091 | Cite as

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

  • I. E. Eliseev
  • A. N. Yudenko
  • N. A. Besedina
  • A. B. Ulitin
  • V. M. Ekimova
  • S. R. Evdokimov
  • J. V. Putintceva
  • P. A. Yakovlev
  • M. I. Lomovskaya
  • I. N. Terterov
  • A. A. Bogdanov
  • M. V. Dubina
Article
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Abstract

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: ΔG = 8.5 kcal mol–1, T m = 76°C, ΔH m = 107 kcal mol–1, ΔC 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.

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Copyright information

© Pleiades Publishing, Ltd. 2017

Authors and Affiliations

  • I. E. Eliseev
    • 1
  • A. N. Yudenko
    • 1
  • N. A. Besedina
    • 1
  • A. B. Ulitin
    • 2
  • V. M. Ekimova
    • 2
  • S. R. Evdokimov
    • 2
  • J. V. Putintceva
    • 2
  • P. A. Yakovlev
    • 2
  • M. I. Lomovskaya
    • 2
  • I. N. Terterov
    • 1
  • A. A. Bogdanov
    • 1
  • M. V. Dubina
    • 3
  1. 1.St. Petersburg National Research Academic UniversityRussian Academy of SciencesSt. PetersburgRussia
  2. 2.CJSC BiocadSt. PetersburgRussia
  3. 3.Pavlov First St. Petersburg State Medical UniversitySt. PetersburgRussia

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