| Literature DB >> 26938670 |
V Celentano1, D Diana1, C Di Salvo1,2, L De Rosa1, A Romanelli3, R Fattorusso4, L D D'Andrea5.
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.Entities:
Keywords: NMR spectroscopy; click chemistry; cycloaddition; peptidomimetics; β-hairpin
Mesh:
Substances:
Year: 2016 PMID: 26938670 DOI: 10.1002/chem.201600154
Source DB: PubMed Journal: Chemistry ISSN: 0947-6539 Impact factor: 5.236