Unprecedented Molecular Architectures by the Controlled Self‐Assembly of a β‐Peptide Foldamer

Abstract

Kampf gegen Windmühlen: Durch die Selbstorganisation eines kurzen helicalen β‐Peptids in wässriger Lösung wurden hochgradig homogene, wohldefinierte und endliche „Windmühlen“ und quadratischen Stäbchen gleichende supramolekulare Architekturen gebildet (siehe Bild). Die reproduzierbare Bildung der neuartigen 3D‐Formen konnte durch den Einsatz unterschiedlicher Konzentrationen eines Tensids gesteuert werden.

A fluorimetric study on the interaction between a Trp‐containing beta‐strand peptide and amphiphilic polymer‐coated gold nanoparticles

“…(B) Diameter distribution analysis of polymer‐coated AuNPs using Image J software (mean diameter 5.6 ± 0.2 nm). (C) Hydrodynamic diameter of AuNPs before and after polymer coating measured by DLS. (D) Zeta‐potential measurements of AuNPs and Pep11 in water.…”

“…Peptides, as viewed as biopolymers by chemists, also provide interesting programmed properties either by themselves, as predesigned nanostructures or as scaffolds for hybrid nanofabrication from inorganic NPs. Amyloid peptides like Amyloid‐beta (A‐beta) , Non‐Amyloid Component (NAC) and GAV are able to self‐assemble into hierarchical nanostructures under special conditions. Despite their pathogenic mechanisms, some of the amyloid fibrillization processes resulting from peptides have been found to be accelerated or inhibited by NPs with different surface chemistries or size/volume properties.…”

“…In addition, extended β‐sheet nanotapes with epitaxial growth on a mica surface make it a perfect model peptide for studying almost all possible nanostructures. To understand the deliberate design of P 11 ‐2, three typical interactions were used: hydrophobic interactions provided by the side chains of Gln, Arg, Glu, Phe and Trp residues; π–π interactions between aromatic moieties of residues Phe4, Trp6 and Phe8; and coulombic attraction between Arg3 and Glu9, which also favours an antiparallel alignment of the strands. Here, the CH 3 CO‐terminus of P 11 ‐2 was altered to NH 2 CO‐ to increase its solubility in aqueous solution and simultaneously keep its termini blocked to avoid edge‐to‐edge coulombic attraction between tapes, as originally designed.…”

Synthesis and Structural Characterization of Homochiral Homo‐oligomers of Parent cis‐ and trans‐Furanoid‐β‐Amino Acids

“…[2] The homo-and heterooligomeric b-peptides have been shown to adopt diverse secondary structures (helices, sheets, and turns) and form interesting molecular architectures by self assembly. [3] The homo-oligomers derived from the conformationally constrained (through ring annulations at the C a ÀC b bond) bamino acids have been the subject of extensive structural investigations. [4][5][6][7] The nature of the secondary structure of their homo-oligomers seems to depend mainly upon 1) the relative stereochemistry of the amine and acid groups, 2) ring atoms, and 3) the ring size.…”

Enhancing β3‐Peptide Bundle Stability by Design

“…The heavy atom-heavy atom distance between bhAsp 12 and bhLys 10 spans 4.0 , well within the 5.0 limit for analogous interactions in proteins containing a-amino acids. [3] There is considerable interest currently in the design of higher-order, nonproteinaceous assemblies possessing defined oligomeric states, [13] as materials with these properties have potential as nanomaterials [14] and catalysts. [15] Here we show that the stability of a b-peptide bundle can be tuned by controlling the length of a solvent-exposed surface salt-bridge interaction.…”