Simulations of the adsorption process of a model-peptide to a zwitterion-lipid bilayer: What can we learn from it?

RODOLFO D. PORASSO; JOSÉ JAVIER LÓPEZ CASCALES; JORGE A. VILA

Tucumán

Congreso; XLI SAB 2012; 2012

SAB

<!-- @page { margin: 2cm } P { margin-bottom: 0.21cm } -->One of the main conclusions of a recently published manuscript,1 about adsorption of peptides to a surface, read: ??for the helix stabilization to occur over the ?native? random coil one, the peptide should contain enough amino acids residues with the proper acid/basic character and to be oriented in a favorable way to maximize the interactions with the HA surface?? This result call our attention because it is known, for the last 30 years,2 that the polypeptide adsorption to a surface, induced by either temperature or pH,stabilize the helical, against random-coil, conformations.2,3 Aimed to understand the nature of such conformational preference in biological systems, we decided to revisit it by carrying out a series of simulations of the adsorption process of a model-peptide to a zwitterion-lipid bilayer.