Discovery of a Pseudo β Barrel: Synthesis and Formation by Tiling of Ferrocene Cyclopeptides

Abstract

Selbstorganisation von Cyclopeptiden mit 1,n′‐disubstituierten Ferrocen‐Einheiten ergab die erste Modellverbindung mit β‐Fass‐Struktur, einem allgegenwärtigen Strukturmotiv in Proteinen. Die acht β‐Stränge der Modellverbindung sind annähernd parallel zur Achse eines Kanals mit 8 Å Porendurchmesser ausgerichtet.

How Useful Is Ferrocene as a Scaffold for the Design of β‐Sheet Foldamers?

“…Forcing peptides into a specific conformation by cyclization has led to a H‐bonding pattern that, although not identical, bears some resemblance to what is observed in proteinic β‐sheets, in terms of the formation of H‐bonded rings and peptide dihedral angles. On an intermolecular level, H‐bonding interactions form associated conjugates into unprecedented supramolecular assemblies 9. The key to this success was the use of glycine (Gly) as a flexible amino acid that can accommodate a wide range of dihedral angles proximal to the Fc core.…”

Stimuli‐Responsive Supramolecular Gelation in Ferrocene–Peptide Conjugates

“…[4] Importantly, ferrocene-peptide conjugates have attracted tremendous attention in designing secondary-structure mimics of peptides because these conjugates have the ability to form hierarchical assemblies driven by weak non-covalent interactions. [5] Despite these interesting features, the application of ferrocene-peptide foldamers in forming supramolecular gels has not yet been explored. Herein, we report two novel ferrocene-dipeptide organogelators that are capable of forming gels in various solvents.…”

Bioconjugates of 1′‐Aminoferrocene‐1‐carboxylic Acid with (S)‐3‐Amino‐2‐methylpropanoic Acid and L‐Alanine

“…Usually, these IHBs are sufficiently strong to retain this approximate C 2 symmetrical conformation in chloroform solution. [18][19][20][21][22][23][24][25][26][27][28] Unsymmetrical 1,nЈ-disubstituted ferrocenoyl amides CH 3 O-Phe-Fcd-AA-OCH 3 with AA equalling achiral amino acids Gly, β-Ala or γ-Aba (Phe = phenyl alanine, Gly = glycine, β-Ala = β-alanine, γ-Aba = γ-aminobutyric acid) were shown to exhibit less stable double IHBs the more methylene groups are inserted. [28] Scheme 1.…”