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. 2021 May 19;12:2956. doi: 10.1038/s41467-021-23254-1

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© The Author(s) 2021

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 FPOP analysis of placental CS binding to wild-type DBL1-ID2. 13 chymotryptic peptides in VAR2CSA were found to exhibit significant protection from oxidation upon binding to placental CS (blue asterisks, p < 0.05, two-tailed Student’s t test). Two peptides (red asterisks, p < 0.05, two-tailed Student’s t test) exhibit significant exposure. Peptides not detected as oxidized in either condition are not shown. b SDS-PAGE non-reduced/reduced of DBL1-ID2 wild-type (KKKWIWKK) and mutant (KKKAIAKK). The gel shown is from one purification, the mutant DBL1-ID2 was purified three times and the wild-type protein more than three times. c T_m determination by nanoDSF melting curves of wild-type (T_m 67.7 °C) and mutant (T_m 63.7 °C) DBL1-ID2. Region between 40 °C and 80 °C is shown. d QCM biosensor kinetic measurements of wild-type (top, k_D1 1.1 nM) and mutant DBL1-ID2 (bottom, no binding) to decorin CSPG. e Flow cytometry binding analyses of lung cancer cell line A549 to wild-type and mutant DBL1-ID2. Source data are provided in source data file.