K88 fimbrial adhesin targeting of microspheres containing gentamicin made with albumin glycated with lactose
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The formulation and characterization of gentamicin-loaded microspheres as a delivery system targeting enterotoxigenic Escherichia coli K88 (E. coli K88) was investigated. Glycated albumin with lactose (BSA-glucose-β (4-1) galactose) was used as the microsphere matrix (MS-Lac) and gentamicin included as the transported antibiotic. The proposed target strategy was that exposed galactoses of MS-Lac could be specifically recognized by E. coli K88 adhesins, and the delivery of gentamicin would inhibit bacterial growth. Lactosylated microspheres (MS-Lac1, MS-Lac2 and MS-Lac3) were obtained using a water-in-oil emulsion, containing gentamicin, followed by crosslinking with different concentrations of glutaraldehyde. Electron microscopy displayed spherical particles with a mean size of 10–17 μm. In vitro release of gentamicin from MS-Lac was best fitted to a first order model, and the antibacterial activity of encapsulated and free gentamicin was comparable. MS-Lac treatments were recognized by plant galactose-specific lectins from Ricinus communis and Sophora japonica and by E. coli K88 adhesins. Results indicate MS-Lac1, produced with 4.2 mg/mL of crosslinker, as the best treatment and that lactosylated microsphere are promising platforms to obtain an active, targeted system against E. coli K88 infections. © 2015 by the authors; licensee MDPI, Basel, Switzerland.
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Gentamicin; Lactosylated microspheres; Targeted active drug adhesin; gentamicin; glutaraldehyde; glycosylated albumin; K88 fimbrial adhesin; lactose; lectin; microsphere; unclassified drug; water oil cream; albuminoid; antiinfective agent; bacterial antigen; Escherichia coli protein; fimbria protein; gentamicin; K88 antigen, E coli; plant lectin; protein binding; antibacterial activity; Article; bacterial growth; drug formulation; drug release; drug targeting; entrapment efficiency; enzyme linked immunosorbent assay; Escherichia coli; flow cytometry; growth regulation; in vitro study; minimum inhibitory concentration; nonhuman; optical density; particle size; physical parameters; Ricinus communis; scanning electron microscopy; Sophora japonica; chemistry; drug effects; metabolism; Albumins; Anti-Bacterial Agents; Antigens, Bacterial; Escherichia coli; Escherichia coli Proteins; Fimbriae Proteins; Gentamicins; Lactose; Microspheres; Plant Lectins; Protein Binding
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