Diarylethene moiety as an enthalpy-entropy switch: photoisomerizable stapled peptides for modulating p53/MDM2 interaction

Author:

Strizhak Alexander V.12345,Babii Oleg6789ORCID,Afonin Sergii6789ORCID,Bakanovich Iuliia12345,Pantelejevs Teodors102114,Xu Wenshu1234,Fowler Elaine1234ORCID,Eapen Rohan122134ORCID,Sharma Krishna1234ORCID,Platonov Maxim O.51415ORCID,Hurmach Vasyl V.514151617,Itzhaki Laura122134,Hyvönen Marko102114ORCID,Ulrich Anne S.678918ORCID,Spring David R.1234ORCID,Komarov Igor V.1617151920ORCID

Affiliation:

1. University Chemical Laboratory

2. University of Cambridge

3. CB2 1EW Cambridge

4. UK

5. Enamine Ltd

6. Institute of Biological Interfaces (IBG-2)

7. Karlsruhe Institute of Technology (KIT)

8. 76021 Karlsruhe

9. Germany

10. Department of Biochemistry

11. CB2 1GA Cambridge

12. Department of Pharmacology

13. CB2 1PD Cambridge

14. 02094 Kyiv

15. Ukraine

16. Taras Shevchenko National University of Kyiv

17. 01601 Kyiv

18. Institute of Organic Chemistry (IOC)

19. Lumobiotics GmbH

20. Karlsruhe

Abstract

Photoisomerization of diarylethene-modified peptides changes the thermodynamics of their binding to MDM2: the “closed” photoisomers bind largely due to a high negative enthalpy, whereas the “open” forms bind better due to a more favourable entropy.

Funder

Medical Research Council

Deutsche Forschungsgemeinschaft

H2020 Marie Skłodowska-Curie Actions

Bundesministerium für Bildung und Forschung

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

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