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. 2020 Jan 17;11:336. doi: 10.1038/s41467-019-13654-9

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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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Fig. 2 — a An additional 15 s3Flag-scFv-HA proteins derived from scFvs in supplementary Fig. 2 were constructed, and their aggregation rate in HeLa cells was quantified using immunocytochemical analysis. Statistical correlation analysis of the net negative charge and aggregation rate of 16 s3Flag-scFv-HA proteins including s3Flag-scFv-A36-HA, and scFv-GFPA36 in HeLa cells (17 scFvs were tested) (left, net negative charge at pH 6.6 vs. aggregation rate: r = 0.6168, P = 0.008179; right, net negative charge at pH 7.4 vs. aggregation rate: r = 0.3709, P = 0.1427). The arrow in left panel (pH 6.6) indicates a net charge value of scFv-GFPA36, which is shifted to a higher absolute value of the negative charge in the right panel (pH 7.4), owing to its relatively high pI. The success rate of stable expression (less than around 2% aggregation) of s3Flag-scFv-HA proteins (16 total proteins) was found to be ~82%. b Statistical correlation analysis of pIs and aggregation rates of 17 scFv proteins used in a (r = 0.8392, P = 0.000025). Source data are provided as a Source Data file.