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. 2020 Jul 7;11:3384. doi: 10.1038/s41467-020-17153-0

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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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Fig. 1 — Schematic illustration of a protein and b LPS captured by telodendrimer nanoparticles via the combination of charge and hydrophobic interactions. c–e Agarose gel electrophoresis profiles reveal the complex formation of the FITC-labled LPS with telodendrimer PEG^5k(ArgVE)₄, as indicated by the lost mobility in migration (repeated independently a minimum of twice). c LPS originated from both E. coli and P. aeruginosa can be captured efficiently by the telodendrimer PEG^5k(ArgVE)₄. d PMB form less-stable complex with LPS in electrophoresis, which was also unable to dissociate LPS– PEG^5k(ArgVE)₄ nanocomplex with 40-fold excess in mass ratio. e The stability of LPS–PEG^5k(ArgVE)₄ nanocomplex was also observed to be stable in the presence of serum protein (RB-BSA) at different mass ratios.