Studies on the anti-phospholipase A2 and anti-inflammatory activities of a uteroglobin fragment and related peptides.
The nonapeptide antiflammin P1 (H-Met-Gln-Met-Lys-Lys-Val-Leu-Asp-Ser-OH), its isoAsp8 analogue and the corresponding aminosuccinyl peptide were prepared, characterized and tested for inhibition of phospholipase A2 (PLA2) in vitro and for anti-inflammatory activity in vivo under assay conditions recently recommended. All peptides are devoid of PLA2 inhibitory and anti-inflammatory activity.
Marastoni
M
M
Department of Pharmaceutical Sciences, University of Ferrara, Italy.
Scaranari
V
V
Romualdi
P
P
Donatini
A
A
Ferri
S
S
Tomatis
R
R
D000595:Amino Acid Sequence; D000818:Animals; D000894:Anti-Inflammatory Agents, Non-Steroidal / Q000494:pharmacology*; D002351:Carrageenan; D002851:Chromatography, High Pressure Liquid; D004487:Edema / Q000139:chemically induced / Q000517:prevention & control; D008297:Male; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis / Q000494:pharmacology*; D010741:Phospholipases A / Q000037:antagonists & inhibitors*; D054467:Phospholipases A2; D051381:Rats; D017207:Rats, Sprague-Dawley; D016339:Spectrometry, Mass, Fast Atom Bombardment; D013056:Spectrophotometry, Ultraviolet; D014598:Uteroglobin / Q000032:analysis / Q000494:pharmacology*
D000894:Anti-Inflammatory Agents, Non-Steroidal; D010446:Peptide Fragments; D002351:Carrageenan; D014598:Uteroglobin; D010741:Phospholipases A; D054467:Phospholipases A2