α,ε-Hybrid Peptide Foldamers: Self-Assembly of Peptide with Trans Carbon-Carbon Double Bonds in the Backbone and Its Saturated Analogue.

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ID: 22464
2018
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Abstract
The effect of geometrically rigid trans α,β-unsaturated ε-amino acids on the structure, folding, and assembly of α,ε-hybrid peptide foldamers has been reported. From single-crystal diffraction analysis, the unsaturated tetrapeptide has stapler-pin-like structure but without intramolecular hydrogen bond. The asymmetric unit has two molecules that are stabilized by multiple intermolecular hydrogen bonding interactions as well as π-π stacking interactions between the aromatic rings of 3-aminocinnamic acid. Peptide does not form organogel. But on hydrogenation, peptide provides the saturated α,ε-hybrid peptide foldamer , which forms instant gel in most of the aromatic solvents. The gel exhibits high stability. The unsaturated peptide has porous microsphere morphology, but saturated analogue has ribbonlike morphology. The gel has been used efficiently for removal of cationic organic pollutants from waste water.
Reference Key
debnath2018hybridacs Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Debnath, Mintu;Das, Tanmay;Podder, Debasish;Haldar, Debasish;
Journal ACS omega
Year 2018
DOI
10.1021/acsomega.8b00832
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Keywords Keywords not found

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