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Preparation and Characterization of Poly (D,L-Lactide-Co-Glycolide) Microspheres for Controlled Release of KSL Peptide
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The purpose of this research was to prepare, characterize, and evaluate the new antimicrobial peptide  KSL peptide encapsulated in poly(D,L-lactide-co-glycolide) (PLGA)composite microspheres. KSL was loaded in poly(acryloyl hydroxyethyl) starch (acHES) micropar-ticles, and then the peptide-containing microparticles were encapsulated in the PLGA matrix by a solvent extraction /evaporation method.

 KSL-loaded PLGA microspheres were also prepared without the starch hydrogel microparticle microspheres for comparison study. KSL peptide microspheres were characterized for drug content, surface morphology, microspheres size determination, polymers stability , in vitro microspheres degradation and in vitro release. KSL peptide encapsulation efficiency resulted in about 98% for RG503 microspheres and AcHES- RG503 composite microspheres. Microspheres mean diameters were 11.12μm  and 28μm for RG503 microspheres and AcHES- -RG503 composite microspheres respectively. Differential scanning calorimetry (DSC) analysis showed no structural changes in the polymers after KSL peptide loading.  The morphological effects and polymers degradation were analyzed to obtain a better understanding of the mechanism of KSL peptide release from microspheres and composite microspheres. Microspheres incubated in 0.1M phosphate buffer saline, pH 7.4 at 37°C were hydrated and started to degrade as shown by gel permeation chromatography (GPC) analysis. The result indicated that the release of KSL peptide from microspheres was due to the bulk degradation.  In vitro release profile showed that the microspheres type significantly affect the release of KSL peptide. In vitro KSL peptide release after 60 days incubation in 0.1M phosphate buffer saline, pH 7.4 at 37°C were 82.23% and 62.12% from 10% KSL peptide loaded AcHES-RG503 composite microspheres and 10%KSL peptide loaded RG503 microspheres respectively.

  Key words :KSL peptide  , microspheres, composite microspheres,  PLGA

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Publication Date
Tue Aug 02 2011
Journal Name
J. College Of Education / Al-mustansiriya University
Synthesis and characterization of mixed ligand complexes of some metals with ( L- phenylalanine and nicotinamide)
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This paper presents the synthesis and study of some new mixed-ligand complexes containing nicotinamide(C6H7N2O) symbolized (NA) and phenylalanine (C9H11NO2)symbolized (pheH)] with some metal ions. The resulting products were found to be solid crystalline complexes which have been characterized by :Melting points, Solubility, Molar conductivity. determination the percentage of the metal in the complexes by flame(AAS), magnetic susceptipibility, Spectroscopic Method [FT-IR and UV-Vis]. The proposed structure of the complexes using program , chem office 3D(2006) . The general formula have been given for the prepared complexes : [M(NA)2(phe)]cl M(II): Mn(II) ,Co(II) , Ni(II) , Cu(II) , Zn(II) , Cd(II) & Hg(II)). NA = Nicotinamide= C6

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Publication Date
Sun Jan 01 2012
Journal Name
Al-mustansiriya J. College Of Education
Synthesis and characterization of mixed ligand complexes of some metals with ( L- phenylalanine and nicotinamide)
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This paper presents the synthesis and study of some new mixed-liagnd complexes containing nicotinamide(C6H7N2O) symbolized (NA) and phenylalanine (C9H11NO2)symbolized (pheH)] with some metal ions. The resulting products were found to be solid crystalline complexes which have been characterized by :Melting points, Solubility, Molar conductivity. determination the percentage of the metal in the complexes by flame(AAS), magnetic susceptipibility, Spectroscopic Method [FT-IR and UV-Vis]. The proposed structure of the complexes using program , chem office 3D(2006) . The general formula have been given for the prepared complexes :[M(NA)2(phe)]cl M(II): Mn(II) ,Co(II) , Ni(II) , Cu(II) , Zn(II) , Cd(II) & Hg(II) . NA = Nicotinamide= C6H7N2O Phe -

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Publication Date
Sun Dec 06 2009
Journal Name
Baghdad Science Journal
Purification and Characterization of protease from Zahdi dates plam seeds (Phoenix dactylifera L.)
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Proteinases (E.C.3.4.21) family are widely distributed in the nature; it was present in animals tissues , plants and microbial cell . Protease was purified from Zahdi seed (Phoenix dactylifera L.) by several steps included ammonium sulphite ppt (75%) saturation and dialyzed against the 80mM sodium phosphate buffer at pH 7.5 . The enzyme specific activity was 407.62 unit/mg protein. The obtained extract was purified by DEAE-Cellulose column followed by gel filtration through Sephacyl S-200 column .The enzyme specific activity ,yield and purification fold were 1873.49 unit/mg protein, 22.99 and 58.42% respectively. The results of protease characterization showed that the molecular weight was 25118 daltons as determined by gel f

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Publication Date
Mon Oct 01 2018
Journal Name
Journal Of Engineering
Synthesis and Characterization of Magnetic Iron Oxide Nanoparticles by Co-Precipitation Method at Different Conditions
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Magnetic nanoparticles (MNPs) of iron oxide (Fe3O4) represent the most promising materials in many applications. MNPs have been synthesized by co-precipitation of ferric and ferrous ions in alkaline solution. Two methods of synthesis were conducted with different parameters, such as temperature (25 and 80 ̊C), adding a base to the reactants and the opposite process, and using nitrogen as an inert gas. The product of the first method (MNPs-1) and the second method (MNPs-2) were characterized by x-ray diffractometer (XRD), Zeta Potential, atomic force microscope (AFM) and scanning electron microscope (SEM). AFM results showed convergent particle size of (MNPs-1) and (MNPs-2) with (86.01) and (74.14)

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Publication Date
Fri Jan 01 2021
Journal Name
Aip Conference Proceedings
Preparation and characterization of mawsonite Cu6Fe2SnS8 [CFTS] thin films via the semi-computerized spray pyrolysis technique for photovoltaic applications
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Publication Date
Fri Jan 01 2021
Journal Name
Aip Conference Proceedings
Preparation and characterization of biomass-alumina composite as adsorbent for safranine-o dye from aqueous solution at different temperatures
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Publication Date
Wed Jul 03 2013
Journal Name
Eur. Chem. Bull
PREPARATION AND CHARACTERIZATION OF UNSATURATED POLYESTER MATERIAL BLENDED WITH CELLULOSE AND WITH ETHYL CELLULOSE.
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Modified unsaturated polyester (MUPE) was blended with Cellulose (Cls) and with ethyl cellulose (ECls) at ambient conditions in the presence of ethyl methyl ketone peroxide (EMKP) as hardener. The blends containing different weight percentages (5-25 %) of Cls or ECls. Mechanical properties (impact strength, hardness, and bending) and dielectric constant were determined. The results observed that Cls increases the impact strength, hardness, and dielectric constant and decreases the bending of the MUPS, while ECls causes an increase in the three mechanical behaviours and a decrease in the dielectric constant of the MU-PS.

Publication Date
Wed Jan 01 2020
Journal Name
Iraqi Journal Of Applied Physics
Preparation and Characterization of Anatase Titanium Dioxide Nanostructures as Smart and Self-Cleaned Surfaces
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Publication Date
Sun Feb 27 2022
Journal Name
Iranian Journal Of Ichthyology
Production of peptide antibiotic bacteriocin using banana peel media
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Many strains of lactic bacteria produce antimicrobial peptides of bacteriocins that are antibiotics used against pathogenic strains. The present work aimed to use a banana peels medium in the fermentation process to replace the commercial MRS medium for decreasing the cost of bacteriocins LAB production. Based on the result, banana peel was a cost-effective and viable alternative carbon source for the production and development of bacteriocin-producing Lactobacilli. The growth of lactobacilli in commercial MRS medium and Banana Peel medium showed no differences, therefore banana peel waste can be used to produce Lactobacilli bacteriocins. Lactobacillus strains grew exceptionally well at 37 C and pH 6.0.

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Publication Date
Mon Aug 14 2017
Journal Name
Oriental Journal Of Chemistry
Leucine Aminopeptidase from Arachis hypogaea L. Seeds Partial Purification and Characterization
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Leucine amino peptidases (LAP; EC 3.4.11.1) constitute a diverse set of exopeptidases that catalyze the hydrolysis of leucine residues from the amino-terminal of protein or peptide substrates, (LAP) are present in animals, plants, and microbes. In this study, leucine amino peptidase was purified partial from Arachis hypogaea seeds by using gel filtration chromatography Sephadex G-100. The enzyme was purified 3.965 fold with a recovery of 29.4%. Its pH and temperature optimum were(8.7) and (37oC), respectively. The results show novel properties of LAP from Arachis hypogaea L. or peanut. The Km value for LAP (77 mM), with V max (1538 m mole min-1). We recommend a separate isoenzymeof the enzyme (LAP) from Arachis hypogaea on L. peanut seeds a

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