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. 2019 Oct 29;10:4777. doi: 10.1038/s41467-019-11984-2

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© The Author(s) 2019

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. 1 — Development of ProCA32.collagen1 and its biophysical characteristics. a The model structure and development of ProCA32.collagen1 by engineering collagen type I targeting moiety (GGGKKWHCYTYFPHHYCVYG, red) at C-terminal of ProCA32 using a flexible hinge (green) and PEGylation. b Measurement of the dissociation constant of ProCA32.collagen1 to collagen type I using indirect ELISA assay. No collagen I binding was observed for ProCA32 (PEGylated, nontargeted agent). c The relaxation rates change of clinical contrast agents (black diamond Eovist; black circle Magnevist; white square MultiHance; white triangle Omniscan; blue square ProHance; yellow circle Dotarem) and red lozenge ProCA32.collagen1 in the presence of ZnCl₂ at different time points up to 4 days. d Pharmacokinetic of ProCA32.collagen1. Gd³⁺ concentration in serum collected after injection of ProCA32.collagen1 was determined by ICP-OES. Error bars indicate standard deviations of six separate measurements in n = 6, biologically independent animals