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. 2022 Apr 7;12:5904. doi: 10.1038/s41598-022-09574-2

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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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The methodology of the high-throughput (HTP) holdup (HU) assay. (Panel A) General sequence of the foldamer library members and structure of H14 helix in side and plan view generated manually by Schrödinger Maestro 11.7 molecular modelling software. The 256-membered foldamer library was divided into 4 sublibraries (L1–L4) based on the general characteristic of the second amino acid (labelled with red) in the sequence. Each sublibrary consists of 64 individuals (R2: four different amino acids, R5: sixteen different amino acids). These four sublibraries (L1–L4) are aromatic, charged, aliphatic, and polar, respectively. (Panel B) His-tagged S100 proteins immobilized on Co²⁺-resin (left panel) are incubated with the H14 foldamer library (256 members). The unbound fraction (flow-through) is recovered (middle panel) and the flow-through fractions are analyzed by LC–MS.