title: β-Hairpin stabilization through an interstrand triazole bridge.
abstract: β-Hairpin peptides were conformationally stabilized through a 1,4 disubstituted 1,2,3-triazole interstrand linkage. A NMR conformational analysis revealed that the β-hairpin content depends on the number and position of substituent methylene units of the 1,2,3-triazole ring. These results will allow the design of metabolically stable peptidomimetic analogs of bioactive β-hairpin peptides.
authors: Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134, Napoli, Italy.
authors: Veronica
authors: V
authors: Celentano
authors: Donatella
authors: D
authors: Diana
authors: Lucia
authors: L
authors: De Rosa
authors: Alessandra
authors: A
authors: Romanelli
authors: Roberto
authors: R
authors: Fattorusso
authors: Luca Domenico
authors: LD
authors: D'Andrea
mesh_terms: D002626:Chemistry, Pharmaceutical / Q000379:methods*; D009682:Magnetic Resonance Spectroscopy; D008697:Methane / Q000031:analogs & derivatives / Q000737:chemistry; D010455:Peptides / Q000032:analysis / Q000737:chemistry*; D057786:Peptidomimetics / Q000032:analysis / Q000138:chemical synthesis*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000032:analysis / Q000737:chemistry*; D014230:Triazoles / Q000737:chemistry*
chemical_list: D010455:Peptides; D057786:Peptidomimetics; D011506:Proteins; D014230:Triazoles; C539234:Trpzip2 protein; C504223:methylene radical; D008697:Methane