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. 2021 Feb 19;11:4284. doi: 10.1038/s41598-021-83198-w

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© Crown 2021

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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Comparative responses of VHH-IR5 to IGF1R ID fragments. HSQC spectra of ¹⁵N-labelled VHH-IR5 identify effects of interactions with three unlabelled IGF1R ID fragments. In black are the HSQC spectra of free VHH-IR5 collected immediately before additions of Ubi-ID, Ubi-s-ID and Pep5 while superimposed in red are the HSQC spectra of the sdAb complexes at ~ 1:1 molar ratio. (a) spectral comparisons showing the effects of Ubi-ID binding. (b) spectra showing the effects of Ubi-s-ID binding. Note that Ubi-ID (a) and Ubi-s-ID (b) binding induce almost the same perturbations, i.e. disappearances of many HSQC signals of ¹⁵N-labelled VHH-IR5, especially those of residues T51 and I52 at the beginning of the CDR2 loop and many other residues in the framework region. All perturbed residues were labelled using the resonance assignments of ¹⁵N-labelled VHH-IR5 (Fig. S5). (c) Widespread spectral displacements of ¹⁵N-labelled VHH-IR5 were produced by binding of the peptide fragment Pep5.