A Two-Tailed Phosphopeptide Crystallizes to Form a Lamellar Structure

Area of Science:

• Biomolecular chemistry
• Structural biology
• Supramolecular chemistry

Background:

• Amphiphilic peptides mimic phospholipid bilayers, crucial for cellular structures.
• Understanding their self-assembly and molecular organization is key to biomimetic design.

Purpose of the Study:

• To present the high-resolution crystal structure of a designed phospholipid-inspired amphiphilic phosphopeptide.
• To investigate the self-assembly mechanisms and nanostructure formation of this peptide.

Main Methods:

• X-ray crystallography at 0.8 Å resolution to determine the crystal structure.
• Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy to correlate crystal structure with supramolecular nanostructures.

Main Results:

• The phosphopeptide forms a lamellar structure stabilized by hydrogen bonding and aromatic interactions, resembling a phospholipid bilayer.
• Water molecules interact within the hydrophilic region of the phosphopeptide lattice.
• Solid-state NMR confirmed self-assembly into semi-elliptical nanosheets, providing insights into the assembly process.

Conclusions:

• The study provides the first atomic-level view of a two-tailed peptidic bilayer, offering insights into biomimetic amphiphilic peptide organization.
• The findings bridge the gap between atomic structure and macroscopic self-assembly, advancing the design of novel peptide-based materials.