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.