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Conformational Heterogeneity of Cyclosporin A in Cyclophilin 18 Binding

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  • Weilin Lin
  • Andres Quintero
  • Yixin Zhang

Abstract

The immunosuppressive drug cyclosporin A (CsA) binds to its receptor protein cyclophilin 18 (Cyp18) in two distinct kinetic phases, while the mechanism remains elusive. Stopped-flow measurements coupled with titration and competition experiments were used to investigate the puzzling two-phase process of CsA and Cyp18 interaction. This study leads to the dissection of different conformational fractions of either direct fast binding or slow binding with rate-limiting conformational inter-conversion and the real-time measurement of kon value (8.34 ± 0.22 x106 M-1s-1) in solution. Furthermore, our study indicates that the structure of CsA during dissociation from the protein possesses a distribution of conformations different from those in solution under equilibrium condition.

Suggested Citation

  • Weilin Lin & Andres Quintero & Yixin Zhang, 2016. "Conformational Heterogeneity of Cyclosporin A in Cyclophilin 18 Binding," PLOS ONE, Public Library of Science, vol. 11(4), pages 1-9, April.
    • Handle: RePEc:plo:pone00:0153669
    DOI: 10.1371/journal.pone.0153669
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