vitronectin

Vitronectin, a multifunctional glycoprotein found in blood and the extracellular matrix, interacts with glycosaminoglycans, collagen, plasminogen, and the urokinase-receptor, in addition to stabilizing the inhibitory conformation of plasminogen activation inhibitor-1. It is utilized in research related to wound healing and tumor progression [1].

Vitronectin (367-378), a peptide derived from residues 367-378 of the multifunctional glycoprotein Vitronectin, plays a pivotal role in cell growth, angiogenesis, and metastasis in various human tumors.

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

P11 acetate is an integrin αvβ3-vitronectin interaction antagonist(IC50 = 2.74 nM).

Cilengitide (EMD 121974) is a potent integrin inhibitor for the αvβ3 5 receptor (IC50: 4.1 79 nM, in cell-free assays) with approximately 10-fold selectivity against gpIIbIIIa.

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.

HSDVHK-NH2 TFA acts as an antagonist to the αvβ3-vitronectin integrin interaction, displaying an inhibitory concentration (IC 50) of 1.74 pg/mL (2.414 pM) [1] [2].

Potent antagonist of the integrin αvβ3-vitronectin interaction (IC50 = 25.72 nM). Blocks proliferation and induces apoptosis in HUVECs; antiangiogenic.

RTDLDSLRTYTL is a ligand for αVβ6 integrin, exhibiting selective inhibition of fibronectin's binding to αVβ6 integrin with considerably less effect on the interactions between vitronectin and αVβ3 or αVβ5, as well as fibrinogen and αIIβ3 (IC50s = 0.02, >50, >50, and >50 µM, respectively). Additionally, it prevents HT-29 colon cancer cells from binding to fibronectin in a concentration-dependent fashion.

VnP-16, a synthetic peptide fragment mirroring amino acids 270-281 of vitronectin (a multifunctional glycoprotein involved in cell attachment, migration, and spreading), promotes attachment and spreading of isolated human osteogenic cells. This effect is reversible with β1 integrin siRNA knockdown when VnP-16 is applied at 9.1 µg/cm2 on cell plates. The compound enhances osteogenesis in human skin-derived mesenchymal precursors and MC3T3-E1 mouse calvarial osteoblast precursors. Furthermore, in vivo studies show VnP-16 mitigates IL-1α-induced bone loss, reduces calvarial osteoclast numbers in mice, increases bone mineral density, and lessens trabecular bone loss in a mouse model of ovariectomy-induced bone loss.