Publications by authors named "J Tomasic"

Background: Physicochemical characteristics of liposome/DNA complexes influence transfection efficiency and affect each other in a very intricate way. The result of this is discrepancies in conclusions drawn about the individual influence of each one.

Methods: Aiming to elucidate the influence of liposome/DNA charge ratio and size on transfection efficiency and on each other, we used liposome/DNA complexes with charge ratio (+/-) in the range of 1-50 and extruded through membranes of 400, 200, and 100 nm.

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In this study, spin-labelled ovalbumin (SL-OVA), free or entrapped in liposomes, was administered to mice subcutaneously (s.c.) or intravenously (i.

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Structurally related peptidoglycan monomer (PGM) and muramyl dipeptide (MDP) differ in several aspects of biological activity but have in common immunostimulating properties. Comparative study of the effects of these adjuvants on humoral IgG immune response specific for protein antigen ovalbumin (OVA) was carried out in two inbred mouse strains, CBA and NIH/OlaHsd, and their ability to modulate the bias of immune response towards Th1/Th2 was evaluated. MDP had better adjuvant activity at some points than PGM, whereas both adjuvants stimulated Th2-biased immune response specific for OVA.

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Liposomes, either alone or in combination with additional immunostimulatory molecules, could be used for the delivery of antigens as vaccine adjuvants. The aim of this study was to investigate the influence of (a) composition (fusogenicity and charge) of large multilamellar liposomes, (b) antigen entrapment efficiency into cationic liposomes and (c) addition of immunostimulatory peptidoglycan monomer (PGM) into liposomal formulations on intensity and direction of antigen-specific humoral immune response. Ovalbumin (OVA) was used as a model antigen and liposomal formulations were tested in a well defined experimental mice model.

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The aim of this work was to prepare mannosyl derivatives of peptidoglycan monomer (PGM, beta-d-GlcNAc-(1-->4)-d-MurNAc-l-Ala-d-isoGln-mesoDAP(epsilonNH(2))-d-Ala-d-Ala) in order to study the effects of mannosylation on adjuvant (immunostimulating) activity. Novel Man-OCH(2)CH(CH(3))CO-PGM isomers were substrates for N-acetylmuramyl-l-alanine amidase, like the parent PGM molecule. Adjuvant activity of Man-OCH(2)CH(CH(3))CO-PGM was tested in the mouse model using ovalbumin as an antigen.

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