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. 2018 Dec 5;9:2768. doi: 10.3389/fimmu.2018.02768

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Copyright © 2018 Bülow, Zeller, Werner, Toelge, Holzinger, Entzian, Schubert, Waldow, Gisch, Hammerschmidt and Gessner.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Structural requirements for binding of bLPs to BPI. BPI binding assay (A–F). Lipopeptides with modified structure as well as DAG were tested for their potential to inhibit binding of rBPI to LPS biotin-coated wells (A–F). Absorbance measured at 450 nm for wells with rBPI alone was set to 100% to ensure comparability between the different ligands. All results are shown as means ± SD of at least four biological replicates. R₁ = CH₃(CH₂)₁₄. Electrostatic charge surface of the BPI structure (G). N-terminal lipid-binding pocket surrounded by differently charged areas is depicted with phosphatidylcholine as ligand.