Simulation of the adsortion process of a model-peptide to a zwitterion-lipid bilaye: What can we learn from it?

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

Tucumán

Congreso; XLI Reunión Anual de la Sociedad Argentina de Biofísica; 2012

SAB

One of the main conclusions of a recently published manuscript, 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, that the polypeptide adsorption to a surface, induced by either temperature or pH,stabilize the helical, against random-coil, conformations. 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.