Beta amino acid‐modified and fluorescently labelled kisspeptin analogues with potent KISS1R activity. (June 2016)

• Record Type: Journal Article
• Authors: Camerino, M. A.; Liu, M.; Moriya, S.; Kitahashi, T.; Mahgoub, A.; Mountford, S. J.; Chalmers, D. K.; Soga, T.; Parhar, I. S.; Thompson, P. E.
• Is Part Of: Journal of peptide science. Volume 22:Number 6(2016:Jun.)
• Page Start: 406
• Page End: 414
• Publication Date: 2016-06
• Subjects: kisspeptin -- KISS1R agonist -- beta amino acids -- fluorescent peptides; Peptides -- Periodicals; Peptides -- Periodicals; 572.65
• DOI: 10.1002/psc.2883
• Languages: English
• ISSNs: 1075-2617

Abstract

Abstract : Kisspeptin analogues with improved metabolic stability may represent important ligands in the study of the kisspeptin/KISS1R system and have therapeutic potential. In this paper we assess the activity of known and novel kisspeptin analogues utilising a dual luciferase reporter assay in KISS1R‐transfected HEK293T cells. In general terms the results reflect the outcomes of other assay formats and a number of potent agonists were identified among the analogues, including β 2 ‐hTyr‐modified and fluorescently labelled forms. We also showed, by assaying kisspeptin in the presence of protease inhibitors, that proteolysis of kisspeptin activity within the reporter assay itself may diminish the agonist outputs. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd. Abstract : Known and novel kisspeptin analogues were assayed utilising a dual luciferase reporter assay in KISS1R‐transfected HEK293T cells. β 2 ‐hTyr‐modified and fluorescently labelled analogues were identified as potent KISS1R agonists. Proteolysis may diminish the agonist outputs in the reporter assay.