Heat and mass transfer investigation of rotating hydrocarbons droplet which behaves as a hard sphere

AbstractThe steady state boundary layer equations around rotating pure hydrocarbon droplet are solved numerically. The droplet is simulated to behave as a hard sphere. The transfer equations are discretized using an implicit finite difference method where Thomas algorithm solves the system of algebraic equations. Moreover, dimensionless parameters of heat and mass transfer phenomena around a rotating hexane droplet concluded. The thickness of the boundary layer is unknown for this model and therefore, it is determined. Further, this work proposes correlations of Nusselt and Sherwood numbers for monocomponent hydrocarbon droplets in evaporation. These correlations consider the rotation phenomena and further, the variation of the thermophysical and transport properties in the vapour phase

Simulation of cellular irradiation with the CENBG microbeam line using GEANT4

Light-ion microbeams provide a unique opportunity to irradiate biological samples at the cellular level and to investigate radiobiological effects at low doses of high LET ionising radiation. Since 1998 a single-ion irradiation facility has been developed on the focused horizontal microbeam line of the CENBG 3.5 MV Van de Graaff accelerator. This setup delivers in air single protons and alpha particles of a few MeV onto cultured cells, with a spatial resolution of a few microns, allowing subcellular targeting. In this paper, we present results from the use of the GEANT4 toolkit to simulate cellular irradiation with the CENBG microbeam line, from the entrance to the microprobe up to the cellular medium.Comment: 6 pages, 8 figures, presented at the 2003 IEEE-NSS conference, Portland, OR, USA, October 20-24, 200

The effect of reverse current on the dark properties of photovoltaic solar modules

AbstractForward and reverse dark current-voltage (I-V) and capacitance-voltage (C-V) characteristics of commercial amorphous silicon solar modules, were measured in order to study their performance under the influence of induced reverse currents. Maximum module surface temperatures were directly related to each value of the induced reverse current and in to the amount of current leakage respectively. Microscopic changes as a result of hot spots defects and overheating of the solar module, linked to reverse current effects, were also documented and discussed. Experimental evidence showed that different levels of reverse currents are confirmed to be a major degrading factor affecting the performance, efficiency, and power of solar modules

Biohydrogen production from fermentation of organic waste, storage and applications

open access articleBiohydrogen is a carbon-free alternative energy source, that can be obtained from fermentation of organic waste, biomass-derived sugars, and wastewater. This article reviews the current processes for fermentative biohydrogen production from biomass including its appropriate storage and transport challenges. The review showed that a comparison of fermentation pretreatment methods across the literature is complicated and that fermentability tests are necessary to determine the best combination of pretreatment/feedstock. Operational parameters, such as temperature, pH, macro/micronutrients addition are widely dependent on the type of fermentation and microorganisms used and hence their content need to be tailored to the process. For immobilized cells, the range of hydrogen production rate values reported for granulation processes using mixed microbial cultures, were higher (13–297 mmol H2/L h) than those reported for entrapment (1–115 mmol H2/L h) and adsorption (3–83 mmol H2/L h), suggesting an achievable and sustainable route for full-scale applications. A purification phase is mandatory before the final use of biohydrogens. Sorption techniques and the use of membranes are the most widely used approaches. Pressure swing adsorption has the highest recovery rate (it reaches 96%). In addition, storage of biohydrogen can have several forms with varying storage capacities (depending on the form and/or storage materials used). The transport of biohydrogen often faces technical and economic challenges requiring optimization to contribute to the development of a biohydrogen economy

Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer’s disease

The aggregation of the 42-residue form of the amyloid-β peptide (Aβ42) is a pivotal event in Alzheimer’s disease (AD). The use of chemical kinetics has recently enabled highly accurate quantifications of the effects of small molecules on specific microscopic steps in Aβ42 aggregation. Here, we exploit this approach to develop a rational drug discovery strategy against Aβ42 aggregation that uses as a read-out the changes in the nucleation and elongation rate constants caused by candidate small molecules. We thus identify a pool of compounds that target specific microscopic steps in Aβ42 aggregation. We then test further these small molecules in human cerebrospinal fluid and in a Caenorhabditis elegans model of AD. Our results show that this strategy represents a powerful approach to identify systematically small molecule lead compounds, thus offering an appealing opportunity to reduce the attrition problem in drug discovery

Rational design of a conformation-specific antibody for the quantification of A beta oligomers

The accurate quantification of the amounts of small oligomeric assemblies formed by the amyloid β (Aβ) peptide represents a major challenge in the Alzheimer’s field. There is therefore great interest in the development of methods to specifically detect these oligomers by distinguishing them from larger aggregates. The availability of these methods will enable the development of effective diagnostic and therapeutic interventions for this and other diseases related to protein misfolding and aggregation. We describe here a single-domain antibody able to selectively quantify oligomers of the Aβ peptide in isolation and in complex protein mixtures from animal models of disease

Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism

The onset and progression of numerous protein misfolding diseases are associated with the presence of oligomers formed during the aberrant aggregation of several different proteins, including amyloid-ß (Aß) in Alzheimer’s disease and a-synuclein (aS) in Parkinson’s disease. These small, soluble aggregates are currently major targets for drug discovery. In this study, we show that trodusquemine, a naturally-occurring aminosterol, markedly reduces the cytotoxicity of aS, Aß and HypF-N oligomers to human neuroblastoma cells by displacing the oligomers from cell membranes in the absence of any substantial morphological and structural changes to the oligomers. These results indicate that the reduced toxicity results from a mechanism that is common to oligomers from different proteins, shed light on the origin of the toxicity of the most deleterious species associated with protein aggregation and suggest that aminosterols have the therapeutically-relevant potential to protect cells from the oligomer-induced cytotoxicity associated with numerous protein misfolding diseases

Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism

10 pags., 5 figs.The onset and progression of numerous protein misfolding diseases are associated with the presence of oligomers formed during the aberrant aggregation of several different proteins, including amyloid-β (Aβ) in Alzheimer’s disease and α-synuclein (αS) in Parkinson’s disease. These small, soluble aggregates are currently major targets for drug discovery. In this study, we show that trodusquemine, a naturally-occurring aminosterol, markedly reduces the cytotoxicity of αS, Aβ and HypF-N oligomers to human neuroblastoma cells by displacing the oligomers from cell membranes in the absence of any substantial morphological and structural changes to the oligomers. These results indicate that the reduced toxicity results from a mechanism that is common to oligomers from different proteins, shed light on the origin of the toxicity of the most deleterious species associated with protein aggregation and suggest that aminosterols have the therapeutically-relevant potential to protect cells from the oligomer-induced cytotoxicity associated with numerous protein misfolding diseases.This work was supported by the Cambridge Centre for Misfolding Diseases (R.L., B.M., F.S.R., C.K.X., M.P., S.C., S.W.C., J.H., T.K., J.R.K., T.P.J.K., M.V., and C.M.D.), the UK Biotechnology and Biochemical Sciences Research Council (M.V. and C.M.D.), the Wellcome Trust (203249/Z/16/Z to T.P.J.K and M.V.), the Frances and Augustus Newman Foundation (T.P.J.K.), the Regione Toscana – FAS Salute, project SUPREMAL (R.C., A.B., C.C., and F.C.), the Gates Cambridge Trust and St. John’s College Cambridge (R.L.), Darwin College Cambridge (F.S.R.), the Herchel Smith Fund (C.K.X.), a Faculty Development Research Fund grant from the United States Military Academy, West Point (R.L.) and a DTRA Service Academy Research Initiative grant (HDTRA1033862 to R.L.)