Trigramin, an RGD-containing peptide from snake venom, inhibits cell-substratum adhesion of human melanoma cells.
Trigramin, a cysteine-rich, RGD-containing peptide isolated from the venom of the Trimeresurus gramineus snake, inhibited the adhesion of human melanoma cells to fibronectin and fibrinogen. Compared on a molar basis to GRGDSP, trigramin was approximately 500 times more potent than the hexapeptide at inhibiting cell adhesion to fibronectin. The activity of trigramin was abolished by chemical reduction of the molecule, indicating that the secondary structure is important to the biological activity. Trigramin presents an example of an effective inhibitor of cell adhesion that has developed in nature and may prove to be a useful probe in studying the cell surface receptors involved in cell adhesion.
D002448:Cell Adhesion / Q000187:drug effects*; D002478:Cells, Cultured; D005340:Fibrinogen / Q000037:antagonists & inhibitors; D005353:Fibronectins; D006801:Humans; D016023:Integrins; D036341:Intercellular Signaling Peptides and Proteins; D008545:Melanoma / Q000378:metabolism / Q000473:pathology*; D008562:Membrane Glycoproteins / Q000378:metabolism; D008858:Microscopy, Phase-Contrast; D009842:Oligopeptides / Q000378:metabolism; D010455:Peptides / Q000494:pharmacology*; D012910:Snake Venoms / Q000032:analysis
D005353:Fibronectins; D016023:Integrins; D036341:Intercellular Signaling Peptides and Proteins; D008562:Membrane Glycoproteins; D009842:Oligopeptides; D010455:Peptides; D012910:Snake Venoms; C054194:trigramin; C047981:arginyl-glycyl-aspartic acid; D005340:Fibrinogen