Triazolo-β-aza-ε-amino acid and its aromatic analogue as novel scaffolds for β-turn peptidomimetics
| Autor: | Subhendu Sekhar Bag, Subhashis Jana, Afsana Yashmeen, Suranjan De |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
chemistry.chemical_classification
Molecular Structure Peptidomimetic Stereochemistry Metals and Alloys General Chemistry Tripeptide Molecular Dynamics Simulation Triazoles Hydrocarbons Aromatic Pentapeptide repeat Catalysis Surfaces Coatings and Films Electronic Optical and Magnetic Materials Amino acid Folding (chemistry) Turn (biochemistry) chemistry.chemical_compound chemistry Materials Chemistry Ceramics and Composites Aromatic amino acids Peptidomimetics Amino Acids Chirality (chemistry) |
| Zdroj: | Chemical Communications. 51:5242-5245 |
| ISSN: | 1364-548X 1359-7345 |
| DOI: | 10.1039/c4cc08414d |
| Popis: | Triazolo-β-aza-ε-amino acid and its aromatic analogue ((Al)TAA/(Ar)TAA) in the peptide backbone mark a novel class of conformationally constrained molecular scaffolds to induce β-turn conformations. This was demonstrated for (Al)TAA 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, (Ar)TAA, which in a short tripeptide backbone acted as a β-turn mimic as a β-sheet folding nucleator. |
| Databáze: | OpenAIRE |
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