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. 2018 Oct 2;8:14662. doi: 10.1038/s41598-018-33044-3

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© The Author(s) 2018

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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Time resolved frequency (i) and dissipation (ii) monitoring of the Ca²⁺ dependent and reversible lipid binding and membrane bridging/linking by WT AnxA2 (A) and the N-terminal deletion mutants AnxA2 Δ 32 (B) and AnxA2 Δ14 (C) in the QCM-D setup. Numbers illustrate the sequential addition of lipids and proteins: Step 1, SLB formation by SUV adsorption and rupture; step 2, adsorption of the respective AnxA2 derivative; step 3, secondary vesicle application in the form of LUVs; step 4, release of all Ca²⁺-dependently bound material by chelation with EGTA. Models representing the respective experimental setup are shown below the QCM-D recordings (iii). Shown are representative examples of typical experiments carried out n = 12 independent times with at least three different protein batches and vesicle preparations.