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. 2020 Jan 27;10:1194. doi: 10.1038/s41598-019-57279-w

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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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Reactivity of phage-displayed mutated variants derived from nimotuzumab Fab. Purified phage particles were tested by ELISA on polyvinyl chloride microtiter plates coated with the recombinant protein comprising the extracellular region of human EGF receptor. Bound phages were detected with an anti-M13 mAb conjugated to horseradish peroxidase. Selected variants having mutations only in CDR2 (V1-V6) are represented in (A), while variants with replacements in both CDR1 and CDR2 (V7-V11) are shown in (B). Two new variants constructed by combining some of the selected mutations are represented in (C). The original nimotuzumab-derived phage-displayed fragment (Fab-nimo) was included as reference (dotted line). Dilutions of phage samples were calculated to reach equivalent concentrations of all the displayed proteins (display units/mL) according to a previous ELISA on polyvinyl chloride microtiter plates coated with the anti-tag antibody 9E10 to measure display levels.