| Autor: |
Zamarreño F; a Departamento de Física, Grupo de Biofísica - UNS , IFISUR, Universidad Nacional del Sur, CONICET , Bahía Blanca , Argentina., Giorgetti A; b Department of Biotechnology, Faculty of Mathematical , Physical and Natural Sciences, University of Verona , Verona , Italy., Amundarain MJ; a Departamento de Física, Grupo de Biofísica - UNS , IFISUR, Universidad Nacional del Sur, CONICET , Bahía Blanca , Argentina., Viso JF; a Departamento de Física, Grupo de Biofísica - UNS , IFISUR, Universidad Nacional del Sur, CONICET , Bahía Blanca , Argentina., Córsico B; c Facultad de Ciencias Médicas, Instituto de Investigaciones Bioquímicas de La Plata (CONICET-UNLP) , Universidad Nacional de La Plata , La Plata , Argentina., Costabel MD; a Departamento de Física, Grupo de Biofísica - UNS , IFISUR, Universidad Nacional del Sur, CONICET , Bahía Blanca , Argentina. |
| Abstrakt: |
Based on the analysis of the mechanism of ligand transfer to membranes employing in vitro methods, Fatty Acid Binding Protein (FABP) family has been divided in two subgroups: collisional and diffusional FABPs. Although the collisional mechanism has been well characterized employing in vitro methods, the structural features responsible for the difference between collisional and diffusional mechanisms remain uncertain. In this work, we have identified the amino acids putatively responsible for the interaction with membranes of both, collisional and diffusional, subgroups of FABPs. Moreover, we show how specific changes in FABPs' structure could change the mechanism of interaction with membranes. We have computed protein-membrane interaction energies for members of each subgroup of the family, and performed Molecular Dynamics simulations that have shown different configurations for the initial interaction between FABPs and membranes. In order to generalize our hypothesis, we extended the electrostatic and bioinformatics analysis over FABPs of different mammalian genus. Also, our methodological approach could be used for other systems involving protein-membrane interactions. |
