Interaction of recombinant human lactoferrin and SARS-CoV-2 virus to heparin-protein conjugate

The advantages of the complex recombinant human lactoferrin (rhLF) with europium ions have been used to establish quantitative parameters specific interaction rhLF immobilized heparin-protein conjugate as a model cell-surface heparan sulfate proteoglycans. Heparin coupled through terminal formyl by reductive amination an inert protein was adsorbed part in wells polystyrene microplate. rhLF–Eu3+ obtained from native contains 0.8 mol lanthanide ion per (40 % saturation level). Equilibrium heterophase binding system is established within 1 min at room temperature, and calculated association constant rhLF-heparin 2.1 × 107 M–1. reversible saturable character labeled Eu3+ active site heparin confirmed transition into liquid phase when 1000-fold molar excess unlabeled added system. Based on affinity for glycosaminoglycan, blocking effect this SARS-CoV-2 virus that imitates proteoglycan host cell surface revealed. Pretreatment solution (10 µg well) reduces 100 ng viral particles well approximately 80 %. presented results allow one, particular, evaluate integrity structure activity possible substance food supplements pharmaceuticals may be useful developing combined drugs corona infection.