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. 2017 Jul 20;7:5949. doi: 10.1038/s41598-017-06377-8

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© The Author(s) 2017

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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Sequence and cartoon representation of Affibody molecules selected as Aβ₄₂cc protofibril binders. (a) Sequences of the top 25 selected Affibody molecules. The underlined amino acid positions are randomized in the phage display selection. The helical secondary structures are represented in boxes. The Affibody molecules chosen for further characterization are highlighted in blue. From 744 randomly picked clones, the sequence of Z_{Aβ42cc_1} was identified eight times, Z_{Aβ42cc_2} and Z_{Aβ42cc_3} one time, Z_{Aβ42cc_4} eight times and Z_{Aβ42cc_5} three times. (b) The original Z-domain scaffold. Side chains of residues that are subjected to variation in the phage library are indicated. (c) Representation of side chains that are mutated in binder Z_A _β _{42cc_1}. The chemical properties of the side chains of the selected binders group into three chemically distinct regions of the surface, which identifies a ‘positive-nonpolar-polar’ recognition surface pattern.