INTERACTION OF FATTY ACID BINDING PROTEINS (FABPS) WITH ARTIFICIAL MEMBRANES

GISELA FRANCHINI, LISANDRO FALOMIR, LISANDRO LABORDE, HORACIO A. GARDA, JUDITH STORCH AND BETINA CORSICO.

Buenos Aires Argentina

Congreso; XIV Congreso Internacional de Biofísica.; 2002

IUPAB

In this work we have analysed the interaction of intestinal and liver FABP (I and LFABP) with artificial membranes of different composition employing a photoactivable reagent (125I-TID-PC). Apo- and holo-I and LFABP were incubated with vesicles of different composition. We observe that the interaction of IFABP with negatively charged vesicles is higher compared to LFABP, the opposite is seen with zwiterionic vesicles, and both proteins show a higher interaction with membranes in their apo-form. These results are in agreement with our previous observations related to the collisional mechanism of transfer of FA from IFABP to artificial membranes, and the role of electrostatic interactions in the process. The higher interaction observed in absence of the ligand is possibly indicating a higher capacity for FA uptake. The identification of the region or regions involved in the interaction of these proteins with membranes, constitutes our next goal.