Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
The structure was elucidated in this paperNCBI PubMed ID: 28507467Publication DOI: 10.17179/excli2016-804Journal NLM ID: 101299402Publisher: Mainz: University of Mainz
Correspondence: rsharma
iul.ac.in
Institutions: Department of Biosciences, Integral University, Lucknow, India, Pharmaceutics Division, CSIR-Central Drug Research Institute, Lucknow, India
β-glucan particles (GP) are polymeric carbohydrates, mainly found as components of cell wall fungi, yeast, bacteria and also in cereals such as barley and oat, and have been recently shown to have application in macrophage-targeted drug delivery. The aim of this study was to prepare and characterize GP containing a large payload of Rifabutin (RB), an anti-tuberculosis drug effective against MDR-TB at lower MIC than Rifampicin. GP were prepared from yeast cells by acidic and alkaline extraction were either spray dried or lyophilized, prior to RB loading and alginate sealing. The FTIR and 13C-NMR spectra of the GP confirmed a β-(1→3) linked glucan structure, with a triple-helical conformation. The spray dried GP exhibited better characteristics in terms of uniformity, size range (2.9 to 6.1 µm) and more than 75 % particles were below 3.5 μm. The RP-HPLC analysis of spray dried GP revealed drug entrapment and drug loading up to 81.46 ± 4.9 % and ~40.5 ± 1.9 %, respectively, as compared to those dried by lyophilization. Electron microscopy showed nearly spherical and porous nature of GP, and the presence of drug 'nanoprecipitates' filling the pore spaces. The formulation showed adequate thermal stability for pharmaceutical application. The particles were readily phagocytosed by macrophage(s) within 5 min of exposure. Drug release occurred in a sustained manner via diffusion, as the release kinetics best fit for drug release was obtained using Higuchi's equation. Thus, the spray dried GP-based-formulation technology holds promise for enhanced targeted delivery of anti-TB drug(s) to macrophage within a therapeutic window for the clearance of intracellular bacteria.
phagocytosis, macrophage, glucan particles, rifabutin, spray drying, targeted drug delivery
Structure type: homopolymer
Location inside paper: β-glucan particles, GP, p. 218
Trivial name: glucan, β-1,3-glucan, curdlan, curdlan-type polysaccharide 13140, paramylon, curdlan, laminarin, β-glucan, curdlan, β-(1,3)-glucan, β-(1,3)-glucan, curdlan, curdlan, β-1,3-glucan, paramylon, reserve polysaccharide, b-glucan, β-1,3-D-glucan, laminaran, botryosphaeran, laminaran type β-D-glucan, latiglucan I, pachymaran, Curdlan, zymosan A, β-glucan, curdlan, laminarin, zymosan, zymosan, glucan particles, zymosan, β-(1-3)-glucan, β-(1,3)-glucan, β-(1,3)glucan, pachymaran, D-glucan (DPn)540, pachyman, laminaran, curdlan, zymosan, zymosan, β-(1,3)-glucan, zymosan A, zymosan, β-1,3-glucan, curdlan, β-1,3-glucan, curdlan, β-1,3-glucan, curdlan, pachyman, β-(1,3)-glucan, curdlan, callose, a water-insoluble β-(1→3)-glucan, fermentum β-polysaccharide, water-insoluble glucan, callose, laminarin, alkali-soluble β-glucan (PeA3), alkali-soluble polysaccharide (PCAP)
Compound class: EPS, O-polysaccharide, cell wall polysaccharide, lipophosphoglycan, glycoprotein, LPG, glucan, cell wall glucan, polysaccharide, glycoside, β-glucan, β-1, 3-glucan
Contained glycoepitopes: IEDB_1397514,IEDB_142488,IEDB_146664,IEDB_153543,IEDB_158555,IEDB_161166,IEDB_558869,IEDB_857743,IEDB_983931,SB_192
Methods: FTIR, HPLC, extraction, zeta potential measurement, transmission electron microscopy, cell growth, 13C-NMR, immunofluorescent labelling, TG-DTA
Biological activity: high drug loading obtained in the spray dried particles of GP, GP can act as Mϕ targeting carriers to deliver the loaded drug molecules within NIH3T3, AD293, HeLa, and Caco-2 phagocytic cells known to harbor TB bacilli, in vitro release data from the GP-RB-Alg offers hope for the controlled release of the loaded antibiotics over a few days within the Mycobacteria infected Mϕ
Comments, role: 13C NMR analysis of glucan in solid state was recorded, the degree of β-1,6 branching of (1-3)β-D-glucan is reported to be as low as 0.003 due to observation of small 69.3 ppm 13C NMR signal (C6*), NMR temperature was not specified
3D data: conformation data
NCBI Taxonomy refs (TaxIDs): 4932Reference(s) to other database(s): GTC:G51056AN, GlycomeDB:
157, CCSD:
50049, CBank-STR:4225, CA-RN: 51052-65-4, GenDB:FJ3380871.1
Show glycosyltransferases
[as TSV]
13C NMR data:
Linkage Residue C1 C2 C3 C4 C5 C6
bDGlcp 105.62 87.19 78.74 76.47 70.17 63.07
1H NMR data:
missing...
13C NMR data:
| Linkage | Residue | C1 | C2 | C3 | C4 | C5 | C6 |
|---|
| | bDGlcp | 105.62 | 87.19 | 78.74 | 76.47 | 70.17 | 63.07 |
|
There is only one chemically distinct structure:
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