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. 2022 Jul 27;12:12828. doi: 10.1038/s41598-022-16914-9

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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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Spike protein binding to three or one peptide per DNA nanostructure. (A) Results from the switchSENSE measurements of the dissociation constants K_D for the binding interaction of “SARS-CoV-2 S protein” and “SARS-CoV-2 S protein, active trimer” by Acro Biosystems to the monovalent peptide presenting DNA (single SBP1) and the trimeric peptide presenting DNA structure (4-arm SBP1). Trimeric peptide presentation reduces the dissociation constant by a third compared to the monovalent peptide presentation. The “SARS-CoV-2 S protein, active trimer” binds more strongly than the “SARS-CoV-2 S protein”, presumably due to variations in glycosylation and amino acid sequence variations. (B) Results from ELISA for a control, immobilized DNA with one peptide or three peptides and subsequent binding analysis of the “SARS-CoV-2 S protein, active trimer”. Here as well the trimeric presentation results in a significant increase of the signal compared to the monovalent peptide presentation. Although the experiment was repeated multiple times, the results shown here come from one well plate to allow for comparability.