A Two-Tailed Phosphopeptide Crystallizes to Form a Lamellar Structure

Michal Pellach; Sudipta Mondal; Karl Harlos; Deni Mance; Marc Baldus; Ehud Gazit; Linda J.W. Shimon

doi:10.1002/anie.201609877

A Two-Tailed Phosphopeptide Crystallizes to Form a Lamellar Structure

Michal Pellach, Sudipta Mondal, Karl Harlos, Deni Mance, Marc Baldus, Ehud Gazit, Linda J.W. Shimon

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

The crystal structure of a designed phospholipid-inspired amphiphilic phosphopeptide at 0.8 Å resolution is presented. The phosphorylated β-hairpin peptide crystallizes to form a lamellar structure that is stabilized by intra- and intermolecular hydrogen bonding, including an extended β-sheet structure, as well as aromatic interactions. This first reported crystal structure of a two-tailed peptidic bilayer reveals similarities in thickness to a typical phospholipid bilayer. However, water molecules interact with the phosphopeptide in the hydrophilic region of the lattice. Additionally, solid-state NMR was used to demonstrate correlation between the crystal structure and supramolecular nanostructures. The phosphopeptide was shown to self-assemble into semi-elliptical nanosheets, and solid-state NMR provides insight into the self-assembly mechanisms. This work brings a new dimension to the structural study of biomimetic amphiphilic peptides with determination of molecular organization at the atomic level.

Original language	English
Pages (from-to)	3252-3255
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	56
Issue number	12
DOIs	https://doi.org/10.1002/anie.201609877
State	Published - 13 Mar 2017
Externally published	Yes

Bibliographical note

Publisher Copyright:
© 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim

Funding

We thank Diamond Light Source for beamtime (proposal mx10627) and the staff of beamline I03 for assistance with data collection. This work was supported by the Medical Research Council (MRC, UK), the Wellcome Trust by providing administrative support (grant 090532/Z/09/Z). The authors acknowledge the support of employees and the use of experimental resources of Instruct, a Landmark ESFRI project. The solid-state NMR experiments were supported by NWO (grants 700.10.344 and 700.58.102 to M.B.) This project has received funding from the European Research Council (ERC) under the European Union's Horizon 2020 research and innovation programme (grant agreement No BISON-694426 to E.G). We thank Sigal Rencus-Lazar for her valuable comments and suggestions.

Funders	Funder number
Wellcome Trust	090532/Z/09/Z
Horizon 2020 Framework Programme
Medical Research Council
European Commission
Nederlandse Organisatie voor Wetenschappelijk Onderzoek	700.10.344, 700.58.102
Horizon 2020	694426

Keywords

X-ray crystallography
membrane mimetics
peptides
self-assembly
supramolecular chemistry

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10.1002/anie.201609877

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abstract = "The crystal structure of a designed phospholipid-inspired amphiphilic phosphopeptide at 0.8 {\AA} resolution is presented. The phosphorylated β-hairpin peptide crystallizes to form a lamellar structure that is stabilized by intra- and intermolecular hydrogen bonding, including an extended β-sheet structure, as well as aromatic interactions. This first reported crystal structure of a two-tailed peptidic bilayer reveals similarities in thickness to a typical phospholipid bilayer. However, water molecules interact with the phosphopeptide in the hydrophilic region of the lattice. Additionally, solid-state NMR was used to demonstrate correlation between the crystal structure and supramolecular nanostructures. The phosphopeptide was shown to self-assemble into semi-elliptical nanosheets, and solid-state NMR provides insight into the self-assembly mechanisms. This work brings a new dimension to the structural study of biomimetic amphiphilic peptides with determination of molecular organization at the atomic level.",

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AU - Gazit, Ehud

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A Two-Tailed Phosphopeptide Crystallizes to Form a Lamellar Structure

Abstract

Bibliographical note

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