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1.
Pharm Dev Technol ; 27(2): 202-214, 2022 Feb.
Article in English | MEDLINE | ID: mdl-35084279

ABSTRACT

The evidence of cannabis exhibiting polypharmacological properties has been accumulating for the past few decades, particularly for its analgesic and anti-inflammatory abilities. However, inconsistent dosage forms and erratic absorption levels prevent medicinal cannabis products from becoming mainstream recommendations for pain management. Current cannabis products fail to address the undesirable characteristics associated with cannabinoids such as low solubility, poor bioavailability, and lack of specificity, all of which contribute to low therapeutic effect. In this narrative view, the pharmacokinetics of cannabis products and possible methods of drug delivery, in the form of carrier systems, will be explored. The incorporation of cannabinoids into carrier systems provides an opportunity to improve absorption levels, increase bioavailability and reduce adverse events allowing for a greater therapeutic effect.


Subject(s)
Cannabinoids , Cannabis , Medical Marijuana , Analgesics , Anti-Inflammatory Agents , Cannabinoids/pharmacokinetics , Cannabinoids/therapeutic use , Medical Marijuana/therapeutic use
2.
Pharm Dev Technol ; 26(4): 390-402, 2021 Apr.
Article in English | MEDLINE | ID: mdl-33461379

ABSTRACT

Conventional methods of probiotics delivery to farmed aquatic animals are not efficient due to loss of probiotic's viability before the probiotics can reach their site of action. This study aims to develop a microencapsulated probiotic delivery system for black-footed abalone (Haliotis iris). An emulsion technique was used to encapsulate probiotic bacteria within chitosan-coated alginate microparticles (CALG). The efficacy of CALG microparticles in delivering probiotics to abalone was assessed using ex vivo and in vivo experiments. Microparticles (113 ± 4 µm) with encapsulation efficiency of more than 75% were developed using an internal gelation formulation approach. The ex vivo release experiments revealed the lack of probiotic discharge in the first 6 h of incubating CALG in seawater followed by a slight bacterial release within the next 20 h. The exposure of CALG microparticles to simulated gastric and intestinal media showed a significantly higher release of encapsulated bacteria in the simulated intestinal medium. The results of feeding trial revealed that the number of probiotic bacteria in probiotic-fed abalone was significantly higher than the one in the control animals. The results suggest that CALG microparticles can be used as a controlled release system for delivering viable probiotic bacteria to the gastrointestinal tract of abalone.


Subject(s)
Alginates/chemistry , Chitosan/chemistry , Microspheres , Probiotics/administration & dosage , Animals , Emulsions , Gastrointestinal Tract/metabolism , Gastropoda , Seawater , Time Factors
3.
Biotechnol Prog ; 33(2): 549-557, 2017 03.
Article in English | MEDLINE | ID: mdl-27860432

ABSTRACT

Macrobrachium rosenbergii nodavirus (MrNV) is a virus native to giant freshwater prawn. Recombinant MrNV capsid protein has been produced in Escherichia coli, which self-assembled into virus-like particles (VLPs). However, this recombinant protein is unstable, degrading and forming heterogenous VLPs. In this study, MrNV capsid protein was produced in insect Spodoptera frugiperda (Sf9) cells through a baculovirus system. Dynamic light scattering (DLS) and transmission electron microscopy (TEM) revealed that the recombinant protein produced by the insect cells self-assembled into highly stable, homogenous VLPs each of approximately 40 nm in diameter. Enzyme-linked immunosorbent assay (ELISA) showed that the VLPs produced in Sf9 cells were highly antigenic and comparable to those produced in E. coli. In addition, the Sf9 produced VLPs were highly stable across a wide pH range (2-12). Interestingly, the Sf9 produced VLPs contained DNA of approximately 48 kilo base pairs and RNA molecules. This study is the first report on the production and characterization of MrNV VLPs produced in a eukaryotic system. The MrNV VLPs produced in Sf9 cells were about 10 nm bigger and had a uniform morphology compared with the VLPs produced in E. coli. The insect cell production system provides a good source of MrNV VLPs for structural and immunological studies as well as for host-pathogen interaction studies. © 2016 American Institute of Chemical Engineers Biotechnol. Prog., 33:549-557, 2017.


Subject(s)
Escherichia coli/metabolism , Nodaviridae/metabolism , Palaemonidae/virology , Sf9 Cells/metabolism , Vaccines, Virus-Like Particle/biosynthesis , Vaccines, Virus-Like Particle/chemistry , Animals , Cells, Cultured , Cloning, Molecular/methods , Escherichia coli/genetics , Nodaviridae/genetics , Recombinant Proteins/chemistry , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Species Specificity , Spodoptera , Vaccines, Virus-Like Particle/genetics
4.
Biotechnol Prog ; 32(1): 171-7, 2016.
Article in English | MEDLINE | ID: mdl-26519022

ABSTRACT

Nipah virus (NiV) causes fatal respiratory illness and encephalitis in humans and animals. The matrix (M) protein of NiV plays an important role in the viral assembly and budding process. Thus, an access to the NiV M protein is vital to the design of viral antigens as diagnostic reagents. In this study, recombinant DNA technology was successfully adopted in the cloning and expression of NiV M protein. A recombinant expression cassette (baculovirus expression vector) was used to encode an N-terminally His-tagged NiV M protein in insect cells. A time-course study demonstrated that the highest yield of recombinant M protein (400-500 µg) was expressed from 107 infected cells 3 days after infection. A single-step purification method based on metal ion affinity chromatography was established to purify the NiV M protein, which successfully yielded a purity level of 95.67% and a purification factor of 3.39. The Western blotting and enzyme-linked immunosorbent assay (ELISA) showed that the purified recombinant M protein (48 kDa) was antigenic and reacted strongly with the serum of a NiV infected pig.


Subject(s)
Nipah Virus/chemistry , Recombinant Proteins/biosynthesis , Viral Matrix Proteins/biosynthesis , Animals , Baculoviridae/genetics , Enzyme-Linked Immunosorbent Assay , Genetic Vectors , Humans , Insecta/cytology , Nipah Virus/immunology , Recombinant Proteins/genetics , Recombinant Proteins/isolation & purification , Swine/immunology , Swine/virology , Viral Matrix Proteins/genetics , Viral Matrix Proteins/isolation & purification
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