Multimethodological study of non classical FABPs interactions with biological membranes. Evidence of a third mechanism.

FERNANDO ZAMARREÑO; JUAN FRANCISCO VISO; MARÍA JULIA AMUNDARAIN; MARINA IBÁÑEZ-SHIMABUKURU; BETINA CÓRSICO; MARCELO DANIEL COSTABEL

Sierra de la Ventana

Congreso; XLIII Reunión Anual de la Sociedad Argentina de Biofísica; 2014

Universidad Nacional del Sur

Fatty Acid Binding Proteins (FABPs) belongs to a family of intracellular lipid binding proteins with the general function of lipid trafficking. A significant amount of In vivo and in silico studies have shown that different FABPs transfer fatty acids to membranes by two different mechanisms: collisional or difusional [1,2]. Nevertheless, a small group of FABPs with structural features, such as As-p18 from parasitic nematode Ascaris suum [3] and human myelin peripheral membrane protein P2 [4], shows a different behavior. In this work we show that this group of FABPs has an ambiguous behavior in its interaction with biological anionic membranes with a putative third mechanism that seems to be a merger between collisional and difusional mechanisms. In order to study the insights of this unusual protein-membrane interaction, we analyzed the electrostatic involved in the system and developed a bioinformatics study to determinate plausible structure conservation.