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

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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.

Journal

  • Bioorganic & medicinal chemistry letters

    Bioorganic & medicinal chemistry letters 23(9), 2628-2631, 2013-05

    Elsevier Ltd.

Codes

  • NII Article ID (NAID)
    120005244679
  • NII NACSIS-CAT ID (NCID)
    AA1079577X
  • Text Lang
    ENG
  • Article Type
    journal article
  • ISSN
    1464-3405
  • Data Source
    IR 
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