The unprecedented cyclotetrapeptide 2, c[D-Asp-1-amide-betaAla-D-Trp-Phe], shows a nanomolar MOR affinity, albeit deprived of any ionic interaction. 2 Shows a clear D-Trpi+1-Phei+2 beta-turn in solution as well in the receptor-bound state. This compound may represent the lead for novel, atypical liphophilic opioid ligands.
L. Gentilucci, A.Tolomelli, S. Spampinato, A. Bedini, R. De Marco, R. Artali (2010). DETERMINATION OF THE BIOLOGICALLY ACTIVE STRUCTURE OF THE ATYPICAL MOR-LIGAND c[D-Asp-1-amide-beta-Ala-D-Trp-Phe] AND ANALOGUES BY NMR AND MOLECULAR DOCKING.
DETERMINATION OF THE BIOLOGICALLY ACTIVE STRUCTURE OF THE ATYPICAL MOR-LIGAND c[D-Asp-1-amide-beta-Ala-D-Trp-Phe] AND ANALOGUES BY NMR AND MOLECULAR DOCKING
GENTILUCCI, LUCA;TOLOMELLI, ALESSANDRA;SPAMPINATO, SANTI MARIO;BEDINI, ANDREA;DE MARCO, ROSSELLA;
2010
Abstract
The unprecedented cyclotetrapeptide 2, c[D-Asp-1-amide-betaAla-D-Trp-Phe], shows a nanomolar MOR affinity, albeit deprived of any ionic interaction. 2 Shows a clear D-Trpi+1-Phei+2 beta-turn in solution as well in the receptor-bound state. This compound may represent the lead for novel, atypical liphophilic opioid ligands.File in questo prodotto:
Eventuali allegati, non sono esposti
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
