RGDS glycosylated peptides as inhibitors of cell-attachment and platelet aggregation.
Glycopeptides derived from the GRGDS sequence were synthesized to study the effect of the sugar residue on the activity of these peptides. The peptides were tested as inhibitors of cell adhesion to fibronectin and of platelet aggregation. The sugar moiety was found to reduce the biological activity of the parent compounds except for the cyclic derivatives P37 and P38 where the inhibition of platelet aggregation was increased. Some interesting differences were observed between the peptides bearing sugar residues with free hydroxyl groups and those with peracetylated sugars.
Institut Pasteur, Département de Biochimie et Génétique Moléculaire, Paris, France.
E
E
Harth-Fritschy
S
S
Dufour
M
M
Si-Tahar
M
M
Chignard
V
V
Biberovic
D
D
Cantacuzène
D001792:Blood Platelets / Q000187:drug effects; D002236:Carbohydrate Conformation; D002241:Carbohydrates / Q000737:chemistry; D002448:Cell Adhesion / Q000187:drug effects*; D005353:Fibronectins / Q000378:metabolism; D006020:Glycopeptides / Q000138:chemical synthesis*; D006801:Humans; D015394:Molecular Structure; D009842:Oligopeptides / Q000494:pharmacology*; D010456:Peptides, Cyclic / Q000737:chemistry; D010975:Platelet Aggregation Inhibitors / Q000737:chemistry*; D014407:Tumor Cells, Cultured
D002241:Carbohydrates; D005353:Fibronectins; D006020:Glycopeptides; D009842:Oligopeptides; D010456:Peptides, Cyclic; D010975:Platelet Aggregation Inhibitors; C046617:arginyl-glycyl-aspartyl-serine