1,2,3-Triazole Bridge as Conformational Constrain in β-Hairpin Peptides: Analysis of Hydrogen-Bonded Positions
Articolo
Data di Pubblicazione:
2016
Citazione:
1,2,3-Triazole Bridge as Conformational Constrain in β-Hairpin Peptides: Analysis of Hydrogen-Bonded Positions / V. Celentano, D. Diana, C. Di salvo, L. De Rosa, A. Romanelli, R. Fattorusso, L.D. D'Andrea. - In: CHEMISTRY-A EUROPEAN JOURNAL. - ISSN 0947-6539. - 22:16(2016), pp. 5534-5537. [10.1002/chem.201600154]
Abstract:
Conformational constrained β-hairpin peptides are useful tool to modulate protein-protein interactions. A triazole bridge in hydrogen-bonded positions between two antiparallel strands induces a conformational stabilization of the β-hairpin peptide. The entity of the stability of the β-hairpin peptide depends on the length of the bridge.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
click chemistry; cycloaddition; NMR spectroscopy; peptidomimetics; β-hairpin; Amino Acid Sequence; Hydrogen Bonding; Magnetic Resonance Spectroscopy;
Elenco autori:
V. Celentano, D. Diana, C. Di salvo, L. De Rosa, A. Romanelli, R. Fattorusso, L.D. D'Andrea
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