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Development of a selective peptide antagonist for the human natriuretic peptide receptor-B.

Abstract : Activation by C-type natriuretic peptide (CNP) of its receptor NPRB results in venodilation and inhibition of cellular proliferation. NPRB-selective antagonists should be useful to understand their physiological implications. We previously observed that [Thr9,Ser11,Arg16](N,C-ANP)pBNP (P12) is an antagonist for bNPRB and a potent agonist for bNPRA. The antagonist [Ser11](N-CNP,C-ANP)pBNP(2-26) (P18) displays six-fold selectivity towards hNPRB versus hNPRA. Deletion of the C-terminus in [Ser11](N-CNP,C-ANP)pBNP(2-25) (P19) decreases its affinity for hNPRA but improves its selectivity 35-fold. Peptide libraries based on P19 using phage display methodology yielded two positive clones P20 and P21. P19 behaves as the most potent antagonist, but P20 is the most selective.
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https://hal-riip.archives-ouvertes.fr/pasteur-00820035
Contributor : Charles M. Dozois <>
Submitted on : Friday, May 3, 2013 - 1:12:11 AM
Last modification on : Monday, July 20, 2020 - 1:06:04 PM

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Julie Deschênes, Cécile Duperé, Normand Mcnicoll, Nicholas l'Heureux, François Auger, et al.. Development of a selective peptide antagonist for the human natriuretic peptide receptor-B.. Peptides, Elsevier, 2005, 26 (3), pp.517-24. ⟨10.1016/j.peptides.2004.10.017⟩. ⟨pasteur-00820035⟩

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