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. 2022 Aug 30;12:14754. doi: 10.1038/s41598-022-18580-3

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© The Author(s) 2022

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 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/.

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Binding activity of Burosumab variants designed to enhance affinity based on pose27. Four mutations on the light chain were created and tested for binding to wild-type FGF23 using ELISA (a). Only A32S mutations showed 1.6-fold affinity enhancement based on K_d value compared with wild-type Burosumab. V97A, which showed small affinity enhancement (1.2-fold) from alanine scanning promoted the binding affinity up to 3.7-fold when combined with A32S (b,c,d). VL:A32S is predicted to form a new favorable hydrogen bond formation with Y124 of FGF23 (e). Curves were drawn by GraphPad Prism version 8.4.3. A450 refers to absorbance at 450 nm. Structure was created by PyMOL version 2.2.0.