Molecular Dynamic Simulations of Liver Basic Fatty Acid-Binding Protein (L-FABP) in Lipid Membranes

GUILLERMO MONTICH, MARÍA VERÓNICA NOLAN, MASSIMILIANO PERDUCA, HUGO MÓNACO AND MARCOS VILLARREAL

Bariloche

Congreso; . Reunión Anual de la Sociedad de Biofísica; 2003

Sociedad Argentina de Biofísica

We have performed several molecular dynamics simulations of Lb-FABP in the vicinity of lipid membranes. The different simulations were started with the protein located in the water phase, with none or a few contacts with the lipids. When the membrane was made of the anionic lipid DLPS it was observed that Lb-FABP approaches the membrane and establishes contacts with the phospholpid head groups. At the same time, a conformational change was observed: a beta-hairpin which is distal from the domain that interact with the membrane undergo a partial unfolding with loss of secondary structure. When the membrane was composed of the zwitterionic lipid DPPC, Lb-FABP did not establish contacts with the membrane and no conformational changes were observed as compared with the protein in solution. The partial unfolding induced by the interaction with anionic membranes was in agreement with previous experimental observations [V. Nolan, M. Perduca, H. L. Monaco, B. Maggio and Guillermo G. Montich, Biochim. Biophys. Acta, (2003) 1611 98-106].