Characterization of binding of S-layer protein from lactobacilli on liposomes

HOLLMANN, AXEL; DELFEDERICO, LUCRECIA; DE ANTONI, GRACIELA; DISALVO, ANIBAL; SEMORILE, LILIANA

IGUAZU, ARGENTINA

Congreso; XL Reunión Anual SAIB; 2004

S-layers are isoporous structures composed of a single protein with the ability to assemble into monomolecular arrays either in suspension, at liquid-surface interfaces, on lipid films, on liposomes and on solid supports. Due to these unique features, S-layers have a broad application potential in molecular nanotechnology, nanobiotechnology and biomimetic. The aim of this work was the characterization of binding of S-layer from different lactobacilli on lipidic surfaces. For this study we used two different types of liposomes, one with DPPC, cholesterol and stearylamine and other with soybean lecithin (SL) replacing DPPC. The S-layer proteins were obtained from L. kefir JCM 5818, L. brevis JCM 1059 and L. buchneri ATCC 4005. Binding of S-layer protein on liposomes and particle stability were analysed. Z-potential measures showed the existence of protein-lipid interactions, which are dependent of the incubation time and the S-layer protein source, quantity and formation of self-assembly products. The binding affinity of S-layer proteins was higher on SL- than on DPPC-liposomes. Data obtained in this work agree with previously reported results for another source of S-layer protein. In the development of a future well-defined liposomal system for the attachment or encapsulation of molecules for human application, it is important to use natural components as SL and S-layer protein.