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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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 languageEnglish
Pages (from-to)3252-3255
Number of pages4
JournalAngewandte Chemie - International Edition
Issue number12
StatePublished - 13 Mar 2017


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


Dive into the research topics of 'A Two-Tailed Phosphopeptide Crystallizes to Form a Lamellar Structure'. Together they form a unique fingerprint.

Cite this