Opioid peptides. Partially modified retro-inverso dermorphin analogues. XIII.
We studied the effect of partial retro-inverso modification of a selected peptide bond of dermorphin (H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2) related peptides. The drastic loss of mu-receptor affinity following introduction of retro-inverso peptide bond between Phe1-D-Ala2 in the new peptide analogues, emphasized the importance of this backbone in the dermorphin peptides.
Marastoni
M
M
Dipartimento di Scienze Farmaceutiche, Università di Ferrara, Italy.
Balboni
G
G
Tomatis
R
R
Salvadori
S
S
Borea
P A
PA
Uccelli
L
L
D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000187:drug effects / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D002855:Chromatography, Thin Layer; D004723:Endorphins / Q000138:chemical synthesis*; D020875:Enkephalin, Ala(2)-MePhe(4)-Gly(5)-; D004745:Enkephalins / Q000378:metabolism; D006168:Guinea Pigs; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis*; D018847:Opioid Peptides; D010084:Oxidation-Reduction; D011957:Receptors, Opioid / Q000187:drug effects / Q000378:metabolism
D004723:Endorphins; D004745:Enkephalins; D009842:Oligopeptides; D018847:Opioid Peptides; D011957:Receptors, Opioid; D020875:Enkephalin, Ala(2)-MePhe(4)-Gly(5)-; C030058:dermorphin