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. 2022 Nov 16;13:7013. doi: 10.1038/s41467-022-34629-3

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 5 — Pharmacological characterization of PACAP27 (black), VIP (turquoise) and the chimeric peptides Ala4-PACAP27 (pink) and Gly4-VIP (purple); (a) VPAC1R cAMP production, (b) PAC1R cAMP production and (c) PAC1R competition binding. a, b Left, Concentration–response curves for cAMP production normalized to % PACAP27 response (data are the mean ± SEM from 5 independent experiments); right, pEC₅₀ determined from each individual experiment are shown with mean ± SEM of the 5 independent experiments also shown. c Left, Competition binding measured using nanoBRET with AF568-conjugated PACAP27 probe (30 nM) and Nluc-PAC1R in the absence and presence of competing peptides. Data are normalized to % specific PACAP27-AF568 nanoBRET signal (data are the mean ± SEM from 5 independent experiments); right, pIC₅₀ values determined from each individual experiment are displayed with mean ± SEM of the data shown. pEC₅₀ and pIC₅₀ data analysed using one-way ANOVA, Tukey’s post-hoc (ns = not significant, *p < 0.05, **p < 0.01, ****<0.0001). Source data are provided in the Source Data file.