Vitronectin (367-378) is a peptide derived from residues 367-378 of the multifunctional glycoprotein known as Vitronectin. Vitronectin plays a pivotal role in cell growth, angiogenesis, and metastasis within various human tumors.
Aureothricin, a dithiolopyrrolone (DTP) antibiotic originally derived from Streptomyces, demonstrates a broad-spectrum of antibacterial effectiveness. Additionally, it inhibits the adhesion of human umbilical vein endothelial cells (HUVECs) to vitronectin[1].
Variabilin, a novel inhibitor of human platelet aggregation, it is a potent RGD (Arg-Gly-Asp)-containing antagonist of the fibrinogen receptor glycoprotein IIb-IIIa (GPIIb-IIIa; αIIbβ3) and the vitronectin receptor αvβ3.Variabilin is also an antimicrobial furanosesterterpene. Variabilin is an inhibitor of human secretory and cytosolic phospholipase A2 (PLA2) activities that controls eicosanoid production in vitro and in vivo, inhibits neutrophil degranulation and superoxide generation in vitro and shows anti-inflammatory activity after topical or p.o. administration to mice.
Fibrinogen-Binding Peptide (designed by anticomplementarity hypothesis) is a presumptive peptide mimic of the vitronectin binding site on the fibrinogen receptor. Fibrinogen, a soluble plasma protein, serves as a cofactor in platelet activation and is converted.
Potent antagonist of the integrin αvβ3-vitronectin interaction (IC50 = 25.72 nM). Blocks proliferation and induces apoptosis in HUVECs; antiangiogenic.