Urotensin-II peptidomimetic incorporating a non-reducible 1,5-triazole disulfide bond reveals a pseudo-irreversible covalent binding mechanism to the urotensin G-protein coupled receptor-Reference-Cited by-同舟云学术

Urotensin-II peptidomimetic incorporating a non-reducible 1,5-triazole disulfide bond reveals a pseudo-irreversible covalent binding mechanism to the urotensin G-protein coupled receptor

Published:2017 Issue:21 Volume:15 Page:4704-4710
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Pacifico Salvatore¹²³⁴,Kerckhoffs Aidan⁵⁶⁷⁸,Fallow Andrew J.⁹¹⁰⁸,Foreman Rachel E.⁹¹⁰⁸,Guerrini Remo¹²³⁴,McDonald John¹¹¹²¹³⁸,Lambert David G.¹¹¹²¹³⁸,Jamieson Andrew G.⁵⁶⁷⁸^ORCID

Affiliation:

1. Department of Chemical and Pharmaceutical Sciences and LTTA

2. University of Ferrara

3. Ferrara

4. Italy

5. School of Chemistry

6. Joseph Black Building. University Avenue

7. Glasgow

8. UK

9. Department of Chemistry

10. University of Leicester

11. Department of Cardiovascular Sciences

12. Division of Anaesthesia Critical Care & Pain Management

13. Leicester

Abstract

New high affinity peptidomimetic ligands have been developed that provided new insight into the mechanism of binding of U-II peptide with the urotensin-II receptor.

Funder

Leverhulme Trust

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2017/OB/C7OB00959C

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