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. 2021 Nov 17;19:373. doi: 10.1186/s12951-021-01123-9

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© The Author(s) 2021

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. 2 — Preparation and characterization of EVs^−cl−NGF. A Flow cytometry analysis of primary macrophages at 48 h after treatments with IL-4. (Numbers indicated per cent F4/80 + , CD206 + cells). B Western blotting analysis of primary Mø and M2 macrophages. ARG-1 and CD206 was a marker of M2 macrophages. C, D TEM imaging of EVs. E TEM images of EVs^−cl−NGF bound with secondary immune-antibody-linked Au nanoparticles. F CLSM images and the STED images (enlarged illustration in the lower right corner) of EVs^−cl−NGF, EVs (blue) and NGF (green). G The colocalization rate of EVs and NGF. H The size and zeta potentials of EVs before and after loading NGF. I Western blotting analysis of EVs and EVs^−cl−NGF. CD9 and TSG101 was a marker of extracellular vesicles, IL-10 was a functional protein of M2 macrophages, and CCR2 was Inflammatory chemotactic protein. J The release rate of NGF under different conditions (PBS, MMP9 + inhibitor, or MMP9). K Comparison of the activity of NGF released from EVs^−cl−NGF to the original NGF. L, M The stability of particle size and zeta potentials of EVs^−cl−NGF in PBS for 7 days. N, O Before lyophilization and after reconstitution, the particle size and Zeta potential of EVs^−cl−NGF. Data presented the mean ± SD (n = 3 per group) (*P < 0.05, ***P < 0.001 and ns: not significant)