Preparation and in vitro study of hydrochloric norvancomycin encapsulated poly (d,l-lactide-co-glycolide, PLGA) microspheres for potential use in osteomyelitis

Abstract

HNV-loaded PLGA microspheres (HNV-PLGA MSs) were prepared by water-in-oil-in-water (w/o/w) double emulsion solvent evaporation technique. The surface of prepared HNV-PLGA MSs is smooth and nonporous with an average diameter of 69.9 μm. The drug-loading rate and encapsulation rate of HNV-PLGA MSs are 4.40 ± 0.26% and 48.51 ± 14.83%, respectively. Additionally, 43.36% of HNV was released from PLGA MSs after seven days of incubation. The antibacterial effects of HNV released from PLGA were as good as the pure HNV. HNV-loaded PLGA microspheres were successfully prepared using double emulsion solvent evaporation technique and their properties met the requirements for local anti-infection.

Phytol-loaded PLGA nanoparticle as a modulator of Alzheimer’s toxic Aβ peptide aggregation and fibrillation associated with impaired neuronal cell function

“…Acetylthiocholine iodide (ATCI) and butyrylthiocholine iodide (BTCI) (Himedia Laboratories, West Chester, PA, USA) were used as substrates. Ab [25][26][27][28][29][30][31][32][33][34][35] peptides were purchased from GenScript (Piscataway, NJ, USA). All the other chemicals and solvents used in the experiment are of high grade and purity.…”

“…The effect of phytol and encapsulated phytol on the aggregation pattern of Ab peptide was assessed in phase I; parallely, the disaggregation of mature Ab fibrils by phytol and encapsulated phytol was verified in phase II. Freshly prepared 100 lM of Ab [25][26][27][28][29][30][31][32][33][34][35] monomer was incubated in Tris-HCl buffer pH 7.4 at 37 C for 24 h to form oligomers. After the formation of Ab 25-35 oligomer, it was co-incubated with/without of phytol and encapsulated phytol (10 lg/mL) for phase I (24 and 48 h).…”

“…After the formation of Ab 25-35 oligomer, it was co-incubated with/without of phytol and encapsulated phytol (10 lg/mL) for phase I (24 and 48 h). Whereas, for phase II, the freshly prepared Ab [25][26][27][28][29][30][31][32][33][34][35] (100 lM) was incubated for 96 h for the formation of pre-formed Ab [25][26][27][28][29][30][31][32][33][34][35] fibrils. After that, phytol and encapsulated phytol (10 lg/mL) were coincubated with the pre-formed fibrils, and the disaggregation pattern was assessed in 96 h and 9 days.…”

“…The amyloid fibril formation and disaggregation were quantified by Th-T induced fluorescence changes [1]. To determine the amyloid fibril formation, the mixture containing Ab [25][26][27][28][29][30][31][32][33][34][35] with/without phytol and encapsulated phytol (10 mg/mL) were added to 50 mM glycine-NaOH buffer, pH 8.5, containing 5 lM Th-T to a final volume of 300 lL. The assay was measured in triplicate and fluorescence intensities were measured at 450 nm (excitation) and 485 nm (emission) (Molecular Device Spectramax M3, Sunnyvale, CA, USA).…”

“…Alterations in the structural characteristics of Ab [25][26][27][28][29][30][31][32][33][34][35] peptides were analyzed through FT-IR by OMNIC software [19]. The Ab [25][26][27][28][29][30][31][32][33][34][35] peptides (100 lM) were incubated with/without phytol and encapsulated phytol (10 lg/mL) for 24 h, 48 h, 96 h and 9 days. For the analysis, a small ration of the incubated sample was mixed with KBr and then scanned from 1400-1800 cm À1 with a spectral resolution of 4 cm À1 .…”