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. 2019 Apr 15;10:1735. doi: 10.1038/s41467-019-09587-y

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© This is a U.S. government work and not under copyright protection in the U.S.; foreign copyright protection may apply 2019 2019

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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Fig. 2 — Sequences and design of self-assembling peptides (SAPs) and cyclic, enzyme-responsive progelators. a Table of SAPs and progelators based on the (KLDL)₃ and (KFDF)₃ amino acid gelling sequence with corresponding diagrammatical representations (green is progelator sequence, red is recognition sequence, pink is fluorophore). Sequences are shown for the base, unmodified SAPs (KLDL and KFDF) and modified SAPs (KLDL_Linear and KFDF_Linear) primed for cyclization but lacking fluorescent labels, together with the corresponding cyclized versions (progelators, KLDL_Cyclic and KFDF_Cyclic). In addition, rhodamine-labeled modified SAPs (Rho-KLDL_Linear and Rho-KFDF_Linear) are shown, together with their corresponding labeled cyclized progelators (Rho-KLDL_Cyclic and Rho-KFDF_Cyclic). The ‘acm' denotes the acetamidomethyl protecting group on Cysteine residues. ‘Rho' designates the 5(6)-carboxytetramethyl rhodamine label. b, c Modeling predicts β-sheet re-orientation, rather than self-assembly disruption, following significant SAP functionalization. b Predicted structures and ribbon diagrams (bottom) of KLDL and KLDL_Linear SAPs from FibPredictor simulations revealing antiparallel and parallel β-sheet orientations, respectively. c Predicted structures and ribbon diagrams (bottom) of KFDF and KFDF_Linear SAPs from FibPredictor simulations revealing antiparallel and parallel β-sheet orientations, respectively (see Supplementary Tables 1-2). Ball and stick models of interacting peptides are displayed with carbon, oxygen, and nitrogen atoms in white, red, and blue, respectively