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A Two‐Tailed Phosphopeptide Crystallizes to Form a Lamellar Structure
Author(s) -
Pellach Michal,
Mondal Sudipta,
Harlos Karl,
Mance Deni,
Baldus Marc,
Gazit Ehud,
Shimon Linda J. W.
Publication year - 2017
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201609877
Subject(s) - phosphopeptide , lamellar structure , crystallography , bilayer , supramolecular chemistry , amphiphile , hydrogen bond , crystal structure , chemistry , self assembly , intermolecular force , phospholipid , molecule , materials science , peptide , membrane , organic chemistry , biochemistry , copolymer , polymer
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.