In-Silico Characterization of von Willebrand Factor Bound to FVIII

Factor VIII belongs to the coagulation cascade and is expressed as a long pre-protein (mature form, 2351 amino acids long). FVIII deficient or defective in hemophilic A patients, who need be treated with hemoderivatives recombinant substitutes, i.e., biologic drugs. The interaction between von Willebrand factor (VWF) influences pharmacokinetics of medications. In vivo, full-length (FL-FVIII) secreted plasma-inactive which includes B domain, then proteolyzed by thrombin protease activity, leading an inactive plasma intermediate. this work, we analyzed through computational approach binding VWF two structure models (secreted domain-deleted FVIII). We included our analysis atomic model efanesoctocog alfa, novel investigational medication, covalently linked FVIII. carried out structural VWF/FVIII interfaces means protein–protein docking, PISA (Proteins, Interfaces, Structures Assemblies), protein contact networks (PCN) analyses. Accordingly, approaches previously published experimental data demonstrated that domains A3-C1 (BDD-FVIII) preferential site for VWF. Overall, applied topological interface can aimed at rational design drugs other than