StAsp-PSI AFFECTS THE STRUCTURE OF PHOSPHOLIPIDS DURING ITS INTERACTION WITH BIOMEMBRANES

MUÑOZ, F. F.; PALOMARES-JEREZ, F.; DALEO, G. R.; VILLALAIN, J.; GUEVARA, M. G.

Potrero de los Funes, San Luis

Congreso; XLVII Reunión Anual SAIB; 2011

SAIB

We have reported the ability of the swaposin domain of potato aspartic proteases (StAsp-PSI) to produce leakage in vesicle membranes containing anionic phospholipids. However, the mode that StAsp-PSI perturbs the structure of lipidic bilayers is not well understood. Here, we examined the effect of StAsp-PSI on the structural and thermotropic properties of the major phospholipid types of bacterial and animal cells. Results obtained from the steady-state fluorescence anisotropy of the probe DPH showed that StAsp-PSI was able to perturb the lipid acyl chains in anionic membranes, composed of DMPG, DMPS and DMPA.