Conformational constrained b-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 b-hairpin peptide. The entity of the stability of the b-hairpin peptide depends on the length of the bridge.
1,2,3-Triazole Bridge as Conformational Constrain in β-Hairpin Peptides: Analysis of Hydrogen-Bonded Positions / Celentano, V.; Diana, D.; Di salvo, C.; De rosa, L.; Romanelli, Alessandra; Fattorusso, R.; D'Andrea, LUCA DOMENICO. - In: CHEMISTRY-A EUROPEAN JOURNAL. - ISSN 0947-6539. - 22:16(2016), pp. 5534-5537. [10.1002/chem.201600154]
1,2,3-Triazole Bridge as Conformational Constrain in β-Hairpin Peptides: Analysis of Hydrogen-Bonded Positions
Diana, D.;ROMANELLI, ALESSANDRA;D'ANDREA, LUCA DOMENICO
2016
Abstract
Conformational constrained b-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 b-hairpin peptide. The entity of the stability of the b-hairpin peptide depends on the length of the bridge.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
