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.
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]
1,2,3-Triazole Bridge as Conformational Constrain in β-Hairpin Peptides: Analysis of Hydrogen-Bonded Positions
A. Romanelli;
2016
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.
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Chemistry 2016 Celentano_et_al.pdf
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