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. 2021 Jun 13;19:180. doi: 10.1186/s12951-021-00925-1

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© The Author(s) 2021

Open AccessThis 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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 1 — The validation of 2D-HFn and HFn binding to integrin α2β1 assayed with BLI. The integrin α2β1proteins were loaded to the sensor tip from a solution of 10 nM and then incubated with various concentrations of 2D-HFn and HFn in binding buffer with 2 mM Mg²⁺. The association and dissociation binding curves were monitored by eight-channel BLI system Octet RED96 and K_d values were calculated by Octet DataAnalysis software (9.0.0.6.)