Ristocetin A sulfate  (Synonyms: Ristomycin III)

Ristocetin A sulfate (Ristomycin III) is a glycopeptide antibiotic that binds to von Willebrand factor (VWF) and bacterial cell wall components. Ristocetin A sulfate interferes with the biosynthesis of bacterial peptidoglycan by inhibiting transpeptidation. As an inducer of platelet adhesion and aggregation, Ristocetin A sulfate drives conformational changes by binding to the A1 domain of VWF, thereby activating downstream signaling pathways and promoting cytoskeletal rearrangement. Ristocetin A sulfate not only enhances platelet adhesion and spreading on immobilized VWF, but also induces the formation of asymmetric dimers with anticooperativity between platelets and plasma VWF. Ristocetin A sulfate is widely used in studies related to thromboembolic diseases and bacterial infections^[1][2].

Ristocetin A sulfate (1 mg/mL; 10 min, 45 min) induces the formation of intact, smooth lamellipodia and enhances the adhesion of washed human platelets to immobilized VWF; this effect relies on an αᵢᵢbβ₃-dependent, GPIb-independent pathway, and requires PI3-kinase, Src-kinase and intracellular Ca²⁺ signaling, with an average platelet spreading surface area of 41.0 μm^2[1].
Ristocetin A sulfate (1 mg/mL; 900 s) induces rapid, smooth lamellipodial protrusion of human washed platelets on immobilized VWF surfaces; this signaling pathway is dependent on α_IIbβ₃ and independent of GPIb^[1].
Ristocetin A sulfate (1 mg/mL; 45 min) induces the formation of F-actin stress fibers in human washed platelets spread on immobilized VWF, and causes uniform localization of the Arp2/3 complex and talin ^[1].
Ristocetin A sulfate (1 mg/mL; 4 min) significantly enhances the adhesion and spreading of washed human platelets on immobilized VWF under flow conditions, with an average platelet spreading surface area of 40.4 μm², and this process depends on the α_iibβ₃ pathway^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

2150.96

C₉₄H₁₁₀N₈O₄₈S

90831-71-3

Solid

White to off-white

O=C(N[C@H](C(OC)=O)C1=C(C2=C(O)C=CC([C@@H](NC([C@H]3C4=CC(OC5=CC=C([C@@H](O)[C@@H]6C(N[C@H](C(N3)=O)C7=CC(O)=C(C)C(OC8=C(O)C=CC([C@@H](N)C(N6)=O)=C8)=C7)=O)C=C5)=C(O[C@H]9[C@H](O[C@@H]%10[C@@H](O[C@H]%11[C@@H](O)[C@H](O)[C@H](O)CO%11)[C@@H](O)[C@H](O)[C@@H](CO)O%10)[C@@H](O)[C@H](O)[C@@H](CO[C@H]%12[C@H](O)[C@H](O)[C@@H](O)[C@H](C)O%12)O9)C(OC%13=CC=C%14C=C%13)=C4)=O)C(N%15)=O)=C2)C(O[C@H]%16[C@@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O%16)=CC(O)=C1)[C@@H]%15[C@@H]%14O[C@H]%17C[C@@H](N)[C@@H](O)[CH]O%17.OS(O)(=O)=O

Room temperature in continental US; may vary elsewhere.

• [1]. Mccarty O J T, et al. von Willebrand factor mediates platelet spreading through glycoprotein Ib and αIIbβ3 in the presence of botrocetin and ristocetin, respectively[J]. Journal of thrombosis and haemostasis, 2006, 4(6): 1367-1378.

  [2]. Nahoum V, et al. Structure of ristocetin A in complex with a bacterial cell-wall mimetic[J]. Biological Crystallography, 2009, 65(8): 832-838.