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. 2023 Jun 8;7(9):1097–1112. doi: 10.1038/s41551-023-01050-0

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© The Author(s) 2023

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. 3 — a, Schematic overview of apoA1-based fusion protein technology. b, Schematic of apoA1–IL4 fusion protein structure. c,d SDS–PAGE (c) and western blot (d) of recombinantly expressed proteins. Antibodies specific for endogenous IL4 and apoA1. e, Chromatogram and Q-ToF-MS spectrum of apoA1–IL4. f, Kinetics of apoA1–IL4 binding to IL4Rα using SPR. g, Activation of HEK-Blue cells expressing IL4Rα and IL13Rα1 by apoA1–IL4. Data are presented as mean ± s.d. DMPC, 1,2-dimyristoyl-sn-glycero-3-phosphocholine; GGS, glycine–glycine–serine; RU, resonance units.