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. 2020 Jun 2;10:9021. doi: 10.1038/s41598-020-66082-x

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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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Mechanism of biofilm inhibition and dispersal using D-AA. D-AA exhibit anti-eDNA activity. (a) Normal conditions: eDNA forms intercellular bridges by interacting with surface bound positively charged proteins (enolase and GAPDH) via acid-base interactions. (b) Dispersal: addition of anionic D-AA displaces eDNA from the surface bound positively charged proteins. eDNA is released and the intercellular bridges are broken. (c) Inhibition: the present D-AA interact with surface bound positively charged proteins preventing eDNA from associating with these proteins; intercellular bridges are unable to form; eDNA = extracellular DNA; D-AA = D-Aspartic acid and D-Glutamic acid; GAPDH = glyceraldehyde-3-phosphate dehydrogenase.