Ascaris summ´s FABP, As-p18, shows ambiguous behavior in its interaction with biological membranes.

FERNANDO ZAMARREÑO; MARINA IBÁÑEZ-SHIMABUKURO; BETINA CÓRSICO; MARCELO D. COSTABEL

Villa Carlos Paz

Congreso; XLII Reunión Anual de la Sociedad Argentina de Biofísica; 2013

Sociedad Argentina de Biofísica

Fatty Acid Binding Protein (FABP) belongs to a family of intracelular lipid binding proteins with the general function of lipid trafficking. In vivo and in silico studies have shown that different FABPs transfer fatty acids to membranes by two different mechanisms: collisional or difusional. As-p18 is a FABP produced by larvae of parasitic nematode Ascaris suum. Structural features such as extended loops have been observed in this protein. In addition, this protein is secreted to the perivitelline fluid by the third stage larva, showing a unique characteristic for this family. In this work we show that As-p18 has an ambiguous behavior in its interaction with biological anionic membranes with a third mechanism that seems to be a merger between collisional and difusional mechanisms In order to study protein-membrane interaction we analyzed the electrostatic involved in the system, and developed molecular dynamics simulations.