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Cycloheptatriene is a neutral monocyclic unsaturated hydrocarbon that consists of an odd number of carbon atoms and an intervening sp3 carbon in the ring. The three double bonds in the ring correspond to 6 π electrons, which is a Huckel number, and therefore satisfies the criteria of 4n + 2 π electrons. However, the intervening sp3 carbon disrupts the continuous overlap of p orbitals. As a result, cycloheptatriene is not aromatic.
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Structural Polymorphism in a Self-Assembled Tri-Aromatic Peptide System.

Noam Brown1,2, Jiangtao Lei3, Chendi Zhan3

  • 1Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences , Tel Aviv University , Tel Aviv 69978 , Israel.

ACS Nano
|March 21, 2018
PubMed
Summary
This summary is machine-generated.

Carboxybenzyl-protected diphenylalanine (z-FF) self-assembles into diverse nanostructures like nanowires and nanotoroids. This peptide forms beta-sheet structures and self-healing hydrogels, expanding building blocks for nanotechnology.

Keywords:
diphenylalaninepeptide nanotubesself-assemblyself-assembly mechanismstructural polymorphismtoroids

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Area of Science:

  • Peptide self-assembly
  • Nanotechnology
  • Supramolecular chemistry

Background:

  • Peptides are versatile building blocks for self-assembly in nature and nanotechnology.
  • Diphenylalanine (FF) and its derivatives form various nanostructures.
  • Triphenylalanine (FFF) self-assembles into distinct architectures.

Purpose of the Study:

  • To investigate the self-assembly of carboxybenzyl-protected diphenylalanine (z-FF) as a model for triaromatic systems.
  • To understand the effect of triaromatic systems on peptide self-assembly processes.
  • To explore the structural diversity and properties of z-FF nanostructures.

Main Methods:

  • Exploration of self-assembly conditions by varying solvent compositions and peptide concentrations.
  • Generation of a phase diagram for z-FF assemblies.
  • Characterization using X-ray crystallography and secondary structure analysis (e.g., β-sheet conformation).
  • Molecular dynamics (MD) simulations (all-atom and coarse-grained) to analyze conformations and assembly behavior.

Main Results:

  • z-FF self-assembles into diverse nanostructures: nanowires, fibers, nanospheres, and nanotoroids.
  • All assemblies exhibit a β-sheet secondary structure.
  • z-FF forms rigid and self-healing hydrogels in high water ratio solvents.
  • X-ray crystallography reveals a 'wishbone' dimer structure stabilized by methanol-mediated hydrogen bonds.
  • MD simulations confirm crystal structure conformations and replicate experimental assembly outcomes (fibers vs. spheres).

Conclusions:

  • z-FF is a valuable building block for creating diverse peptide-based nanostructures.
  • The study elucidates the self-assembly mechanism and structural features of z-FF.
  • Findings expand the library of peptide building blocks for nanostructure fabrication.
  • The formation of nanotoroids and hydrogels highlights the potential of z-FF in advanced materials applications.