Conformational constrained ?-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 ?-hairpin peptide. The entity of the stability of the ?-hairpin peptide depends on the length of the bridge.

1,2,3-triazole bridge as conformational constrain in ?-hairpin peptides: Analysis of hydrogen-bonded positions

Diana D;DeRosa L;D'Andrea L D
2016

Abstract

Conformational constrained ?-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 ?-hairpin peptide. The entity of the stability of the ?-hairpin peptide depends on the length of the bridge.
2016
Click chemistry
Cycloaddition
NMR spectroscopy
Peptidomimetics
?-hairpin
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Descrizione: 1,2,3-triazole bridge as conformational constrain in ?-hairpin peptides: Analysis of hydrogen-bonded positions
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/313555
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