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. 2024 Sep 17;2(1):33. doi: 10.1038/s44303-024-00037-z

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© The Author(s) 2024

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — a The Eu-DOTAMA-CBP1 probe binds to COL3 with good affinity and specificity. b The FO of the Eu-DOTAMA-CBP1 in the presence of COL3 is 74%. c Competition assay between monomeric Eu-DOTAMA-CBP1 and tetrameric [Gd-DOTAMA]₄-CBP1 shows that the tetramer can displace the monomer from COL3 binding sites. d The Eu-DOTAMA-CBP2 probe binds to COL3 but with a significant non-specific contribution. e The FO of the Eu-DOTAMA-CBP2 in the presence of COL3 is 76% but binding is unspecific. f Competition assay between monomeric Eu-DOTAMA-CBP2 and tetrameric [Gd-DOTAMA]₄-CBP2 shows a small difference between the displacement curves of [Gd-DOTAMA]₄-CBP2 and its scrambled counterpart, suggesting that the binding is largely unspecific. CBP collagen binding peptide, SccCBP scrambled version of the collagen binding peptide, Eu europium, Gd gadolinium, FO fractional occupancy.