The role of mutations in the process of Interaction between FABP- membrane. An Electrostatic study.

FERNANDO ZAMARREÑO; DIEGO F. VALLEJO; AGUSTÍN PICCO; MARCELO D. COSTABEL

Montevideo

Congreso; VI International Conferences of Biological Physics. V Southern Cone Biophysics Congress. XXXIV Annual Meeting of The Argentinean Biophysical Society.; 2007

IUPAP, IUPAB y otras.

The study of reversible protein‑membrane interactions provides insights into cellular physiology, and has a deep impact in biotechnology and medicine. Examples of this kind of proteins are fatty acid binding protein (FABP), sterol carrier protein 2 (SCP2) and acyl‑CoA binding protein (ACBP), all of which have been implicated in processes that facilitate lipid solubilization and movement in the cellular milieu . Intestinal fatty acid binding protein (IFABP) belongs to a family of intracellular lipid binding proteins of low molecular weight (14-15 kD) with the general function of lipid trafficking. The precise physiological functions of these proteins are as yet unclear, but it is hypothesized that they are important in intracellular transport and targeting of FA to specific membranes and metabolic pathways. To get insight into the mechanism of the interaction between FABP and membranes, we modeled the process by computer simulation for FABPs with different mutations. By using the Finite Difference Poisson Boltzmann Equation (FDPB) implemented in the software APBS, we computed the energy involved in the interaction FABP-membrane. We show that binding of FABP to membranes involves a significant electrostatic component that discriminates among possible membrane‑bound models, suggests, in each case, a favored orientation of FABP in the interaction.