59 research outputs found
Techno-economic evaluation of solar irrigation plants installed in Bangladesh
In the summer season, irrigation sector in Bangladesh suffers a lot due to the country wide electricity crisis. Solar pump offers a clean and simple alternative to the conventional fuel fired engine or grid electricity driven pump in this regard to resolve the issue. In this paper, the techno-economic analyses of solar irrigation plants installed in Bangladesh are evaluated. It was observed that systems were running around 70% to 80% of the rated power which was quite acceptable. A 10 hp pump was able to pump 600 liter of water per minute which was also satisfactory to irrigate the land. Average operating time was found to be 8 hour/day. It was found that the overall efficiency of the systems were in between 11.39% to 16.52% whereas the typical average value of lit/Wp/year was 9200. On the other hand, the cost of irrigation to cultivate paddy in 0.161 hectares’ land for one season was 1,750 BDT by solar irrigation which was found to be lower than that of other available modes. This charge for grid electricity based irrigation was about 3,000 to 3500 BDT per 0.161 hectares’ and 2,300 to 2,600 BDT per 0.161 hectares’ for diesel engine based irrigation. According to the current financial scheme (15% equity investment, 35% credit support and remaining 50% from government through IDCOL) the average value of payback period was 5.43 years, NPV in the range from 7 to 15% and IRR was 18%. By considering 100% equity investment, however, these projects were not economically attractive. The payback period for this case was about 18 years. Study also revealed that each solar irrigation plant reduces 42.8 kg of CO2 emission per day compare to diesel engine operated pump and 2566.24 kg/day compared to grid electricity operated pump. A comprehensive effort from the Government as well as from all the stakeholders is required for further expansion of solar irrigation plants in Bangladesh
Modification of structure and properties of well-dispersed dendrimer coated multi-walled carbon nanotube reinforced polyester nanocomposites
This work reveals the structure and properties of dendrimer coated multiwall carbon nanotube (DMWCNT) reinforced unsaturated polyester resin (UPR) nanocomposite. Rheology, as well as the shear thinning behavior of nanosuspension exhibits the dispersion of DMWCNT in UPR matrix. The Raman spectra of DMWCNT-UPR nanocomposites along with the Fourier-transform infrared (FTIR) spectra of DMWCNT and DMWCNT-UPR nanocomposites indicate the interaction between DMWCNT and UPR in the nanocomposite system. Additionally, the surface morphology of DMWCNT and DMWCNT-UPR nanocomposites reveals well dispersion of DMWCNT in DMWCNT-UPR nanocomposites. X-ray diffraction (XRD) profile demonstrates structural properties of pristine UPR and nanocomposites. The Transmission Electron micrograph and Field Emission Scanning Electron micrograph show the fractured surface morphologies of DMWCNT-UPR nanocomposites. Comparative stress-strain behavior shows the deformation mechanism of DMWCNT-UPR nanocomposites
Organotin Antifouling Compounds and Sex-Steroid Nuclear Receptor Perturbation: Some Structural Insights
Organotin compounds (OTCs) are a commercially important group of organometallic compounds of tin used globally as polyvinyl chloride stabilizers and marine antifouling biocides. Worldwide use of OTCs has resulted in their ubiquitous presence in ecosystems across all the continents. OTCs have metabolic and endocrine disrupting effects in marine and terrestrial organisms. Thus, harmful OTCs (tributyltin) have been banned by the International Convention on the Control of Harmful Antifouling Systems since 2008. However, continued manufacturing by non-member countries poses a substantial risk for animal and human health. In this study, structural binding of common commercial OTCs, tributyltin (TBT), dibutyltin (DBT), monobutyltin (MBT), triphenyltin (TPT), diphenyltin (DPT), monophenyltin (MPT), and azocyclotin (ACT) against sex-steroid nuclear receptors, androgen receptor (AR), and estrogen receptors (ERα, ERβ) was performed using molecular docking and MD simulation. TBT, DBT, DPT, and MPT bound deep within the binding sites of AR, ERα, and Erβ, showing good dock score, binding energy and dissociation constants that were comparable to bound native ligands, testosterone and estradiol. The stability of docking complex was shown by MD simulation of organotin/receptor complex with RMSD, RMSF, Rg, and SASA plots showing stable interaction, low deviation, and compactness of the complex. A high commonality (50–100%) of interacting residues of ERα and ERβ for the docked ligands and bound native ligand (estradiol) indicated that the organotin compounds bound in the same binding site of the receptor as the native ligand. The results suggested that organotins may interfere with the natural steroid/receptor binding and perturb steroid signaling
Studies of <img src='http://www.niscair.res.in/jinfo/small.gif' border=0>-α-phosphatidylcholine impregnated parchment paper model membrane
335-339The magnitude of the BIP depends upon the concentration and nature of the cations. Theories based on the principles of irreversible thermodynamics as proposed by Tasaka et al.[J memb Sci, 24 (1985) 29] and Toyosbima et al. [J phys Chern, 74 (1970) 2704] have been compared to obtain a relationship which has been used for the evaluation of theoretical values of bi-ionic potentials. The close agreement between the theoretical and the observed values confirms the applicability of the derived relationship to the membrane- electrolyte systems used in these investigations
Insights into the Endocrine Disrupting Activity of Emerging Non-Phthalate Alternate Plasticizers against Thyroid Hormone Receptor: A Structural Perspective
Many endocrine-disrupting chemicals (EDCs) have a ubiquitous presence in our environment due to anthropogenic activity. These EDCs can disrupt hormone signaling in the human and animal body systems including the very important hypothalamic-pituitary-thyroid (HPT) axis causing adverse health effects. Thyroxine (T4) and triiodothyronine (T3) are hormones of the HPT axis which are essential for regulation of metabolism, heart rate, body temperature, growth, development, etc. In this study, potential endocrine-disrupting activity of the most common phthalate plasticizer, DEHP, and emerging non-phthalate alternate plasticizers, DINCH, ATBC, and DEHA against thyroid hormone receptor (TRα) were characterized. The structural binding characterization of indicated ligands was performed against the TRα ligand binding site employing Schrodinger’s induced fit docking (IFD) approach. The molecular simulations of interactions of the ligands against the residues lining a TRα binding pocket, including bonding interactions, binding energy, docking score, and IFD score were analyzed. In addition, the structural binding characterization of TRα native ligand, T3, was also done for comparative analysis. The results revealed that all ligands were placed stably in the TRα ligand-binding pocket. The binding energy values were highest for DINCH, followed by ATBC, and were higher than the values estimated for TRα native ligand, T3, whereas the values for DEHA and DEHP were similar and comparable to that of T3. This study suggested that all the indicated plasticizers have the potential for thyroid hormone disruption with two alternate plasticizers, DINCH and ATBC, exhibiting higher potential for thyroid dysfunction compared to DEHA and DEHP
Anticancer compound plumbagin and its molecular targets: a structural insight into the inhibitory mechanisms using computational approaches.
Plumbagin (5-hydroxy-2-methyl-1,4-naphthoquinone) is a naphthoquinone derivative from the roots of plant Plumbago zeylanica and belongs to one of the largest and diverse groups of plant metabolites. The anticancer and antiproliferative activities of plumbagin have been observed in animal models as well as in cell cultures. Plumbagin exerts inhibitory effects on multiple cancer-signaling proteins, however, the binding mode and the molecular interactions have not yet been elucidated for most of these protein targets. The present study is the first attempt to provide structural insights into the binding mode of plumbagin to five cancer signaling proteins viz. PI3Kγ, AKT1/PKBα, Bcl-2, NF-κB, and Stat3 using molecular docking and (un)binding simulation analysis. We validated plumbagin docking to these targets with previously known important residues. The study also identified and characterized various novel interacting residues of these targets which mediate the binding of plumbagin. Moreover, the exact modes of inhibition when multiple mode of inhibition existed was also shown. Results indicated that the engaging of these important interacting residues in plumbagin binding leads to inhibition of these cancer-signaling proteins which are key players in the pathogenesis of cancer and thereby ceases the progression of the disease
Computational Insights into the Inhibitory Mechanism of Human AKT1 by an Orally Active Inhibitor, MK-2206
<div><p>The AKT signaling pathway has been identified as an important target for cancer therapy. Among small-molecule inhibitors of AKT that have shown tremendous potential in inhibiting cancer, MK-2206 is a highly potent, selective and orally active allosteric inhibitor. Promising preclinical anticancer results have led to entry of MK-2206 into Phase I/II clinical trials. Despite such importance, the exact binding mechanism and the molecular interactions of MK-2206 with human AKT are not available. The current study investigated the exact binding mode and the molecular interactions of MK-2206 with human AKT isoforms using molecular docking and (un)binding simulation analyses. The study also involved the docking analyses of the structural analogs of MK-2206 to AKT1 and proposed one as better inhibitor. The Dock was used for docking simulations of MK-2206 into the allosteric site of AKT isoforms. The Ligplot+ was used for analyses of polar and hydrophobic interactions between AKT isoforms and the ligands. The MoMa-LigPath web server was used to simulate the ligand (un)binding from the binding site to the surface of the protein. In the docking and (un)binding simulation analyses of MK-2206 with human AKT1, the Trp-80 was the key residue and showed highest decrease in the solvent accessibility, highest number of hydrophobic interactions, and the most consistent involvement in all (un)binding simulation phases. The number of molecular interactions identified and calculated binding energies and dissociation constants from the co-complex structures of these isoforms, clearly explained the varying affinity of MK-2206 towards these isoforms. The (un)binding simulation analyses identified various additional residues which despite being away from the binding site, play important role in initial binding of the ligand. Thus, the docking and (un)binding simulation analyses of MK-2206 with AKT isoforms and its structure analogs will provide a suitable model for studying drug-protein interaction and will help in designing better drugs.</p></div
swoil n; 'seal oil'
seal nHe told me to give her / A cup of old swoil.PRINTED ITEM JUL 1 1988G.M.Story WKUsed I and SupUsed I3Used Isile,soil,swale,swile,swoil(e),bay,harbour,harp,hood,old,square flipper,square a,young,bedlamer,dotard,ragged-jacket,saddleback,turner,white-coat,pelt n,sculp n;~bait/bat/cat/catcher/dart/fat/finger/hunt(er)/gun/hand/heaMore collocations:~hunting/shot/skin(er)/soap/twine/vat/bird/penis/worm/frame/oil/pan/pass/patch;~fish/er(y)/ing;dog1;pup;cock,cod worm;snub1;blow hole;bobbing~;sealer1;fish kille
Potential Disruption of Systemic Hormone Transport by Tobacco Alkaloids Using Computational Approaches
Tobacco/nicotine is one of the most toxic and addictive substances and continues to pose a significant threat to global public health. The harmful effects of smoking/nicotine affect every system in the human body. Nicotine has been associated with effects on endocrine homeostasis in humans such as the imbalance of gonadal steroid hormones, adrenal corticosteroid hormones, and thyroid hormones. The present study was conducted to characterize the structural binding interactions of nicotine and its three important metabolites, cotinine, trans-3′-hydroxycotinine, and 5′-hydroxycotinine, against circulatory hormone carrier proteins, i.e., sex-hormone-binding globulin (SHBG), corticosteroid-binding globulin (CBG), and thyroxine-binding globulin (TBG). Nicotine and its metabolites formed nonbonded contacts and/or hydrogen bonds with amino acid residues of the carrier proteins. For SHBG, Phe-67 and Met-139 were the most important amino acid residues for nicotine ligand binding showing the maximum number of interactions and maximum loss in ASA. For CBG, Trp-371 and Asn-264 were the most important amino acid residues, and for TBG, Ser-23, Leu-269, Lys-270, Asn-273, and Arg-381 were the most important amino acid residues. Most of the amino acid residues of carrier proteins interacting with nicotine ligands showed a commonality with the interacting residues for the native ligands of the proteins. Taken together, the results suggested that nicotine and its three metabolites competed with native ligands for binding to their carrier proteins. Thus, nicotine and its three metabolites may potentially interfere with the binding of testosterone, estradiol, cortisol, progesterone, thyroxine, and triiodothyronine to their carrier proteins and result in the disbalance of their transport and homeostasis in the blood circulation
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