Abstract
Triazolo-β-aza-ε-amino acid and its aromatic analogue (AlTAA/ArTAA) in the peptide backbone mark a novel class of conformationally constrained molecular scaffolds to induce β-turn conformations. This was demonstrated forAlTAA in a Leu-enkephalin analogue and in a designed pentapeptide wherein the FRET process was established. Restricted rotation induced chirality and turn conformation into the achiral aromatic amino acid scaffold,ArTAA, which in a short tripeptide backbone acted as a β-turn mimic as a β-sheet folding nucleator.
Original language | English |
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Pages (from-to) | 5242-5245 |
Number of pages | 4 |
Journal | Chemical Communications |
Volume | 51 |
Issue number | 25 |
DOIs | |
State | Published - 28 Mar 2015 |
Externally published | Yes |
Bibliographical note
Publisher Copyright:© The Royal Society of Chemistry.