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. 2020 Nov 25;21:81. doi: 10.1186/s40360-020-00458-7

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© The Author(s) 2020

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. 7 — The binding interaction of the continentalic acid with various protein target such as p65 (PDB-ID: 1vkx), Nrf2 (PDB-ID: 2flu), Keap1 (PDB-ID: 4iqk), HO-1 (PDB-ID: 1ubb), TNF-α (PDB-ID: 2az5), IL-1β (PDB-ID: 1itb), IL-6 (PDB-ID: 1p9m) and COX-2 (PDB-ID: 5ikq) with their subsequent 3D and 2D structure. The docking analysis was done to calculate the binding energy, vander wall forces and type of binding. The interaction of the continentalic acid with the p65 (a, b), Nrf2 (c, d), Keap1 (e, f), HO-1 (g, h), TNF-α (i, j), IL-1β (k, l), IL-6 (m, n) and COX-2 (o, p) was shown in both 2D and 3D view. The 3D view show the binding pocket within the ligand orient, while the 2D images show the interactive amino acids interacting with the ligand and type of interaction