Characterization of the receptor binding residues of kisspeptins by positional scanning using peptide photoaffinity probes.

Authors

• Ryosuke Misu
• Shinya Oishi
• Shohei Setsuda
• Taro Noguchi
• Masato Kaneda
• Hiroaki Ohno
• Barry Evans
• Jean-Marc Navenot
• Stephen C Peiper
• Nobutaka Fujii

Publication/Presentation Date

5-1-2013

Abstract

Kisspeptins, endogenous peptide ligands for GPR54, play an important role in GnRH secretion. Since in vivo administration of kisspeptins induces increased plasma LH levels, GPR54 agonists hold promise as therapeutic agents for the treatment of hormonal secretion diseases. To facilitate the design of novel potent GPR54 ligands, residues in kisspeptins that involve in the interaction with GPR54 were investigated by kisspeptin-based photoaffinity probes. Herein, we report the design and synthesis of novel kisspeptin-based photoaffinity probes, and the application to crosslinking experiments for GPR54-expressing cells.

Volume

23

Issue

9

First Page

2628

Last Page

2631

ISSN

1464-3405

Published In/Presented At

Misu, R., Oishi, S., Setsuda, S., Noguchi, T., Kaneda, M., Ohno, H., Evans, B., Navenot, J. M., Peiper, S. C., & Fujii, N. (2013). Characterization of the receptor binding residues of kisspeptins by positional scanning using peptide photoaffinity probes. Bioorganic & medicinal chemistry letters, 23(9), 2628–2631. https://doi.org/10.1016/j.bmcl.2013.02.098

Disciplines

Business Administration, Management, and Operations | Health and Medical Administration | Management Sciences and Quantitative Methods

PubMedID

23522565

Department(s)

Administration and Leadership

Document Type

Article