Acyl CoA Binding Protein-Membrane interaction. A Molecular Dynamic study.

NESTOR E. SANCHEZ FORNILLO; FERNANDO ZAMARREÑO; MARCELO D. COSTABEL

Salta

Congreso; XXXIX Annual Meeting of The Argentinean Biophysical Society 2010, Workshop CeBEM & 3rd Latin American Protein Society Meeting.; 2010

SAB, LAPS y otras.

Acyl-CoA binding proteins (ACBPs) are highly conserved 10 kDa cytosolic proteins that bind medium- and long-chain acyl-CoA esters. They act as intracellular carriers of acyl-CoA and play a role in acyl-CoA metabolism, acyl-CoA mediated cell signaling, transport-mediated lipid synthesis, and membrane trafficking. The ACBP binding to anionic phospholipid-rich membranes is similar to that of other intracellular LCFA-CoA binding proteins, in a process where initial recognition could be mainly driven by forces of electrostatic origin and then followed by a variety of events involving protein conformational changes that include the insertion of hydrophobic residues into the membrane. Based in experimental information that reports the interaction of ACBP with phospholipids membranes and proposing an initial configuration for the protein-membrane complex modelled from our electrostatic calculations we performed a Molecular Dynamics simulation of HgACBP-membrane interaction.