An Offset Patterned Cross-β Structure in Assemblies of C3-Symmetric Peptide Amphiphiles

Oleksandr Zagorodko (Corresponding author), Tetiana Melnyk, Vicent J. Nebot, Patricia Y.W. Dankers, María J. Vicent (Corresponding author)

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Abstract

Developing peptide-based materials with controlled morphology is a critical theme of soft matter research. Herein, we report the formation of a novel, patterned cross-β structure formed by self-assembled C3-symmetric peptide amphiphiles based on diphenylalanine and benzene-1,3,5-tricarboxamide (BTA). The cross-β motif is an abundant structural element in amyloid fibrils and aggregates of fibril-forming peptides, including diphenylalanine. The incorporation of topological constraints on one edge of the diphenylalanine fragment limits the number of β-strands in β-sheets and leads to the creation of an unconventional offset-patterned cross-β structure consisting of short 3×2 parallel β-sheets stabilized by phenylalanine zippers. In the reported assembly, two patterned cross-β structures bind parallel arrays of BTA stacks in a superstructure within a single-molecule-thick nanoribbon. In addition to a threefold network of hydrogen bonds in the BTA stack, each molecule becomes simultaneously bound by hydrogen bonds from three β-sheets and four phenylalanine zippers. The diffuse layer of alkyl chains with terminal polar groups prevents the nanoribbons from merging and stabilizes cross-β-structure in water. Our results provide a simple approach to the incorporation of novel patterned cross-β motifs into supramolecular superstructures and shed light on the general mechanism of β-sheet formation in C3-symmetric peptide amphiphiles.

Original languageEnglish
Article numbere202303194
Pages (from-to)e202303194
Number of pages9
JournalChemistry - A European Journal
Volume30
Issue number7
Early online date15 Nov 2023
DOIs
Publication statusPublished - 1 Feb 2024

Funding

The authors acknowledge Stuart P. Atkinson for English editing, and E. Solano and M. Malfois from BL‐11 NCD‐SWEET beamline at ALBA Synchrotron (Spain) for their support with SAXS experiments, and Mario Soriano for his help with (cryo)TEM. The authors thank Marcin Oszajca and Anabel B. González Guillén for their valuable discussions. The authors would like to thank the Spanish Ministerio de Economía y Competitividad (PID2019‐108806RB‐I00), the H2020 European Research Council (grant ERC‐CoG‐2014‐648831 MyNano), the Dutch Ministry of Education, Culture and Science (Gravity Program 024.005.020), and the research program of Chemelot InSciTe (project EyeSciTe) for financial support. T. M. is supported by an AECC Valencia Ph.D. grant. Part of the equipment employed in this work has been funded by Generalitat Valenciana and co‐financed with FEDER funds (PO FEDER of Comunitat Valenciana, 2014–2020).

FundersFunder number
FEDER of Comunitat Valenciana
H2020 European Research CouncilERC‐CoG‐2014‐648831 MyNano
Fundación Científica Asociación Española Contra el Cáncer
Ministerie van Onderwijs, Cultuur en Wetenschap024.005.020
Ministerio de Economía y CompetitividadPID2019‐108806RB‐I00
Generalitat Valenciana

    Keywords

    • benzene-1,3,5-tricarboxamide
    • cross-beta
    • peptide amphiphiles
    • self-assembly
    • supramolecular polymers

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