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. 2017 Jul 25;7:6428. doi: 10.1038/s41598-017-06940-3

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© The Author(s) 2017

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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Inhibition of DsA1 binding to fibrinogen by a peptide derived from the N-terminus of fibrinogen. (a) GST-recombinant proteins (Fg1, Fg2, Fg3, Fg4) were expressed in E. coli (see Supplementary Figs S1 and S2), fractionated by 12.5% SDS-PAGE and detected by Coomassie blue staining. (b) Proteins were probed with biotinylated DsA1 (0.1 μg/ml). (c) Binding activity to hFg (25 μg) with pretreated biotinylated DsA1 with purified recombinant peptides Fg1 (♦), Fg2 (■) or BSA as control (●). Data are presented as the mean ± standard deviation of four independent experiments. Statistical significance is indicated by *P ≤ 0.05, **P ≤ 0.01.