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1,2,3‐Triazole Bridge as Conformational Constrain in β‐Hairpin Peptides: Analysis of Hydrogen‐Bonded Positions
Author(s) -
Celentano V.,
Diana D.,
Di Salvo C.,
De Rosa L.,
Romanelli A.,
Fattorusso R.,
D'Andrea L. D.
Publication year - 2016
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201600154
Subject(s) - antiparallel (mathematics) , peptide , chemistry , bridge (graph theory) , protein structure , crystallography , beta sheet , biophysics , stereochemistry , biochemistry , physics , biology , quantum mechanics , magnetic field , anatomy
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.