lipid-a and betadex

lipid-a has been researched along with betadex* in 1 studies

Other Studies

1 other study(ies) available for lipid-a and betadex

Article	Year
Biologically active lipid A antagonist embedded in a multilayered polyelectrolyte architecture. Biomaterials, 2006, Volume: 27, Issue:9 Recently [Jessel N, Schwinte P, Donohue R, Lavalle P, Boulmedais F, Darcy R, et al. Pyridylamino-beta-cyclodextrin as a molecular chaperone for lipopolysaccharide embedded in a multilayered polyelectrolyte architecture. Adv Funct Mater 2004;14:963-9], we demonstrated the biological activity of a lipopolysaccharide from Escherichia coli incorporated into layer-by-layer films made of poly (l-lysine) and poly (l-glutamic acid) and containing a polycationic beta-cyclodextrin (CD) with chaperone properties. Here we develop innovative architectures containing a complex made of a charged beta-cyclodextrin and a lipid A antagonist (LAA) as potential systems for local endotoxin antagonistic activity. We examine the biological activity of these architectures. The CD-LAA complex adsorbed on top, or embedded into the polyelectrolyte films keeps its LPS antagonistic activity on both murine and human macrophages for at least 24h. Topics: Animals; beta-Cyclodextrins; Cells, Cultured; Humans; Lipid A; Macrophages; Mice; Mice, Inbred C3H; Peptides; Polyamines; Polyelectrolytes; Spectrum Analysis, Raman	2006

Article

Year

Biologically active lipid A antagonist embedded in a multilayered polyelectrolyte architecture.

Biomaterials, 2006, Volume: 27, Issue:9

Recently [Jessel N, Schwinte P, Donohue R, Lavalle P, Boulmedais F, Darcy R, et al. Pyridylamino-beta-cyclodextrin as a molecular chaperone for lipopolysaccharide embedded in a multilayered polyelectrolyte architecture. Adv Funct Mater 2004;14:963-9], we demonstrated the biological activity of a lipopolysaccharide from Escherichia coli incorporated into layer-by-layer films made of poly (l-lysine) and poly (l-glutamic acid) and containing a polycationic beta-cyclodextrin (CD) with chaperone properties. Here we develop innovative architectures containing a complex made of a charged beta-cyclodextrin and a lipid A antagonist (LAA) as potential systems for local endotoxin antagonistic activity. We examine the biological activity of these architectures. The CD-LAA complex adsorbed on top, or embedded into the polyelectrolyte films keeps its LPS antagonistic activity on both murine and human macrophages for at least 24h.

Topics: Animals; beta-Cyclodextrins; Cells, Cultured; Humans; Lipid A; Macrophages; Mice; Mice, Inbred C3H; Peptides; Polyamines; Polyelectrolytes; Spectrum Analysis, Raman

2006