fibrinogen-binding peptide

Fibrinogen-Binding Peptide (designed by anticomplementarity hypothesis) is a presumptive mimic of the vitronectin binding site on the fibrinogen receptor. Fibrinogen, a soluble plasma protein and cofactor in platelet activation, is converted to fibrin in a thrombin-catalyzed reaction.

Fibrinogen-Binding Peptide (designed by anticomplementarity hypothesis) is a presumptive peptide mimic of the vitronectin binding site on the fibrinogen receptor. Fibrinogen-Binding Peptide binds fibrinogen and inhibits both the adhesion of platelets to fibrinogen and platelet aggregation, and also inhibits the adhesion of platelets to vitronectin

Fibrinogen Binding Inhibitor Peptide, a synthetic dodecapeptide, represents the specific platelet receptor recognition site of the human fibrinogen g-chain (residues 400-411).

Arg-Gly-Glu-Ser acetate is a RGD related peptide that is a control for the RGDS activity of fibrinogen binding to activated platelets.

Angstrom6 (A-6 peptide) is an 8 amino acid peptide derived from single chain urokinase fibrinogen activator (scuPA) that interferes with the uPA uPAR cascade and abrogates the downstream effects.Angstrom6 has antitumor activity and inhibits tumor cell migration, invasion, and metastasis by binding to CD44 and modulating CD44-mediated cell signaling.

Arg-Gly-Glu-Ser TFA, an RGD-related peptide, serves as a control for evaluating the inhibitory activity of RGDS on fibrinogen binding to activated platelets.

K-Casein (106-116), bovine, is a peptide that impedes platelet aggregation and fibrinogen binding, significantly contributing to the pathophysiology of atherosclerosis [1].

Arg-Gly-Glu-Ser (RGDS) is an RGD-related peptide used as a control for the activity of fibrinogen binding to activated platelets.