Current Issue : January - March Volume : 2018 Issue Number : 1 Articles : 5 Articles
Biperiden is a drug used in Parkinson disease treatment and it serves also as an antiseizures compound in organophosphates\npoisoning. It acts as antagonist of muscarinic receptor activated by acetylcholine while the enzyme acetylcholinesterase (AChE)\ncleaves acetylcholine in synaptic junction into choline and acetic acid. This enzyme is inhibited by various compounds; however\nthere has not been proposed evidence about interaction with biperiden molecule. We investigated this interaction using standard\nEllman�s assay and experimental findings were critically completed with an in silico prediction by SwissDock docking software.\nUncompetitivemechanismof actionwas revealed fromDixon plot and inhibition constant (...
The emergence of novel pathogenic strains with increased antibacterial resistance patterns poses a significant threat to the\nmanagement of infectious diseases. In this study, we aimed at utilizing the subtractive genomic approach to identify novel drug\ntargets against Salmonella enterica subsp. enterica serovar Poona strain ATCC BAA-1673. We employed in silico bioinformatics\ntools to subtract the strain-specific paralogous and host-specific homologous sequences from the bacterial proteome. The sorted\nproteome was further refined to identify the essential genes in the pathogenic bacterium using the database of essential genes\n(DEG). We carried out metabolic pathway and subcellular location analysis of the essential proteins of the pathogen to elucidate\nthe involvement of these proteins in important cellular processes.We found 52 unique essential proteins in the target proteome that\ncould be utilized as novel targets to design newer drugs. Further, we investigated these proteins in the DrugBank databases and\n11 of the unique essential proteins showed druggability according to the FDA approved drug bank databases with diverse broadspectrum\nproperty. Molecular docking analyses of the novel druggable targets with the drugs were carried out by AutoDock Vina\noption based on scoring functions.The results showed promising candidates for novel drugs against Salmonella infections....
Chloride intracellular channel 1 (CLIC1) is involved in the development of most aggressive human tumors, including gastric, colon,\nlung, liver, and glioblastoma cancers. It has become an attractive new therapeutic target for several types of cancer. In this work, we\naim to identify natural products as potent CLIC1 inhibitors from Traditional Chinese Medicine (TCM) database using structurebased\nvirtual screening and molecular dynamics (MD) simulation. First, structure-based docking was employed to screen the\nrefined TCM database and the top 500 TCM compounds were obtained and reranked by ...
The oxidized low-density lipoprotein receptor-1 (LOX-1) targeted single-chain variable fragment (scFvs) is a promising molecule\nfor the targeted delivery of imaging and therapeutic molecules of atherosclerotic diseases; however, its applications are limited by\nthe inherent low antigen affinity. In this study, the three-dimensional (3D) model of the anti-LOX-1 scFv was constructed and its\ndocking with the LOX-1 protein was developed. To improve the LOX-1-binding activity, the anti-LOX-1 scFv was designed to fuse\nwith one of three LOX-1-binding heptapeptides, LTPATAI, FQTPPQL, and LSIPPKA, at its N-terminus and C-terminus and in\nthe linker region, which have different LOX-1-binding interfaces with the anti-LOX-1 scFv analyzed by an array of computational\napproaches. These scFv/peptide fusions were constructed, successfully expressed in Brevibacillus choshinensis hosts, and purified\nby a two-step column purification process. The antigen binding activity, structural characteristics, thermal stability, and stability in\nserum of these fusion proteins were examined. Results showed that the scFv with N-terminal fusing peptides proteins demonstrated\nincreased LOX-1-binding activity without decrease in stability. These findings will help increase the application efficacy of LOX-1\ntargeting scFv in LOX-1-based therapy....
A thaumatin-like protein gene fromBasrai banana was cloned and expressed in Escherichia coli. Amplified gene product was cloned\ninto pTZ57R/T vector and subcloned into expression vector pET22b(+) and resulting pET22b-basrai TLP construct was introduced\ninto E. coli BL21. Maximum protein expression was obtained at 0.7mM IPTG concentration after 6 hours at 37âË?Ë?C. Western blot\nanalysis showed the presence of approximately 20 kDa protein in induced cells. Basrai antifungal TLP was tried as pharmacological\nagent against fungal disease. Independently Basrai antifungal protein and amphotericin B exhibited their antifungal activity against\nA. fumigatus; however combined effect of both agentsmaximized activity against the pathogen. Docking studies were performed to\nevaluate the antimicrobial potential of TLP against A. fumigatus by probing binding pattern of antifungal protein with plasma\nmembrane ergosterol of targeted fungal strain. Ice crystallization primarily damages frozen food items; however addition of\nantifreeze proteins limits the growth of ice crystal in frozen foods. The potential of Basrai TLP protein, as an antifreezing agent, in\ncontrolling the ice crystal formation in frozen yogurt was also studied.Thescope of this study ranges fromcost effective production\nof pharmaceutics to antifreezing and food preserving agent as well as other real life applications....
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