Oleic Acid interaction with two discrete lipid-binding sites of Ascaris’ ABA-1 nematode polyprotein allergen. A computational analysis.

MACARENA AILEN FERRO; DIEGO OBIOL; MARCELO D. COSTABEL; FERNANDO ZAMARREÑO

Rosario

Congreso; L Reunión Anual de la Sociedad Argentina de Biofísica; 2022

Sociedad Argentina de Biofísica

Atypical lipid-binding proteins such as Nematode polyprotein allergens (NPAs) are foundonly in nematodes. Because of their lack of counterparts in vertebrates and becausehelminthes parasites have a restricted lipid metabolism, NPAs are potential targets fordrug design.ABA-1A is the most common repeating unit of the NPA of Ascaris suum. The aim of thisresearch is to study the interaction between Oleic acid and two previously propousedbinding sites of protein ABA-1A through in silico methods, namely docking and classicmolecular dynamics simulations.To find the most suitable Protein-ligand configurations, we performed a standard flexibledocking simulations through AUTODOCK Vina docking software in each popoused bindingsite. Later, we selected the most suitable configuration based in a scale of relativeinteraction energies as affinity estimators ranked by AUTODOCK Vina. Once one Proteinligand relative position was selected for each putative pocket, they were used as initialconfigurations for MD study of Protein-ligand interaction.ABA-1A – Oleic acid complex was stable during molecular Dynamics simulation.Interaction of Oleic acid with specific residues were noticed in both putatives bindingsites supporting the hypothesis of multiple ligands per protein published in previouswork.