Beta amino acid-modified and fluorescently labelled kisspeptin analogues with potent KISS1R activity

Michelle Camerino; Mengjie Liu; Shogo Moriya; Takashi Kitahashi; A. Mahgoub; Simon Mountford; D. K. Chalmers; Tomoko Soga; Ishwar Parhar; Philip Thompson

doi:10.1002/psc.2883

Beta amino acid-modified and fluorescently labelled kisspeptin analogues with potent KISS1R activity

Michelle Camerino, Mengjie Liu, Shogo Moriya, Takashi Kitahashi, A. Mahgoub, Simon Mountford, D. K. Chalmers, Tomoko Soga, Ishwar Parhar, Philip Thompson

Research output: Contribution to journal › Article › Research › peer-review

7 Citations (Scopus)

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 β2-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.

Original language	English
Pages (from-to)	406-414
Number of pages	9
Journal	Journal of Peptide Science
Volume	22
Issue number	6
DOIs	https://doi.org/10.1002/psc.2883
Publication status	Published - 1 Jun 2016

Keywords

beta amino acids
fluorescent peptides
KISS1R agonist
kisspeptin

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10.1002/psc.2883

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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 β2-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.",

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AU - Camerino, Michelle

AU - Liu, Mengjie

AU - Moriya, Shogo

AU - Kitahashi, Takashi

AU - Mahgoub, A.

AU - Mountford, Simon

AU - Chalmers, D. K.

AU - Soga, Tomoko

AU - Parhar, Ishwar

AU - Thompson, Philip

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AB - 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 β2-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.

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Beta amino acid-modified and fluorescently labelled kisspeptin analogues with potent KISS1R activity

Abstract

Keywords

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