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. 2020 Feb 24;10:3300. doi: 10.1038/s41598-020-60242-9

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© The Author(s) 2020

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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Long chain fatty acids bind with high affinity to AeOBP22. (a) Florescence emission spectra of DAF (blue) excited at 490 nm, with increasing amounts of AeOBP22 (arrow) shows concentration dependent quenching. (b) Titration of the final sample in a, with increasing linoleic acid (arrow) shows that the fatty acid competes for binding of DAF and recovery of initial fluorescence (red). (c) Determination of binding constant for AeOBP22 and DAF from 7 replicates of experiments shown in panel (a). DAF concentration was 84 nM. Plot of the intensity at the florescence maximum (513 nm) presented as change from initial fluorescence. Data were fit according to Eq. 2. (d) Determination of the binding constant of α-linoleic acid at pH 8.0 from multiple replicates (n = 3) of experiments shown in panel (b) by fit of the raw intensity using Eqs. 2 and 3 using a K_D for DAF of 1.191 μM. The DAF concentration was fixed at 100 nM and the protein at 1000 nM. Data are presented as normalized recovery of the quenched fluorescence for ease of viewing. (e) The same experiment as in (d) but recorded at pH 5 (n = 2). Intrinsic DAF fluorescence is significantly quenched at pH 5.0 leading to increased error in measured points.