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1.
J Supercomput ; 79(4): 3643-3665, 2023.
Artículo en Inglés | MEDLINE | ID: mdl-36093387

RESUMEN

This paper presents a prototype filter design using the orthant optimization technique to assist a filter bank multicarrier (FBMC) modulation scheme of a NextG smart e-healthcare network framework. Low latency and very high reliability are one of the main requirements of a real-time e-healthcare system. In recent times, FBMC modulation has gotten more attention due to its spectral efficiency. The characteristics of a filter bank are determined by t's, prototype filter. A prototype filter cannot be designed to achieve an arbitrary time localization (for low latency) and frequency localization (spectral efficiency), as time and frequency spreading are conflicting goals. Hence, an optimum design needed to be achieved. In this paper, a constraint for perfect or nearly perfect reconstruction is formulated for prototype filter design and an orthant-based enriched sparse ℓ1-optimization method is applied to achieve the optimum performance in terms of higher availability of subcarrier spacing for the given requirement of signal-to-interference ratio. Larger subcarrier spacing ensures lower latency and better performance in real-time applications. The proposed FBMC system, based on an optimum design of the prototype filter, also supports a higher data rate as compared to traditional FBMC and OFDM systems, which is another requirement of real-time communication. In this paper, the solution for the different technical issues of physical layer design is provided. The presented modulation scheme through the proposed prototype filter-based FBMC can suppress the side lobe energy of the constituted filters up to large extent without compromising the recovery of the signal at the receiver end. The proposed system provides very high spectral efficiency; it can sacrifice large guard band frequencies to increase the subcarrier spacing to provide low-latency communication to support the real-time e-healthcare network.

2.
Curr Pharm Des ; 20(32): 5212-7, 2014.
Artículo en Inglés | MEDLINE | ID: mdl-24641189

RESUMEN

Glimepiride sulfonamide (GS) is a drug intermediate to synthesize glimepiride (antidiabetic drug). We hypothesized that GS exerts gluco-regulatory effect because GS is comprised of the structural components of dipeptidyl peptidase-IV (DPP-IV) inhibitors sitagliptin and DPP-728and glimepiride (sulfonylurea based antidiabetic drug).We analyzed the drug-likeness and docking efficiency of GS with DPP-IV using in silico tools. Also DPP-IV inhibition assays were conducted in vitro. Gluco-regulatory potential and parameters of drug safety were evaluated on normal euglycemic and streptozotocin (STZ) induced diabetic rats. We observed strong drug-likeness and DPP-IV binding efficiency of GS. Similarly, profound DPP-IV inhibition was also observed in vitro. Studies on euglycemic and STZ induced diabetic rats revealed antidiabetic potential for GS without significant change in the studied toxicological parameters. Glimepiride sulfonamide has antidiabetic potential mainly through DPP-IV inhibition, but also through insulin stimulation and alpha-amylase inhibition.


Asunto(s)
Diabetes Mellitus Experimental/tratamiento farmacológico , Hipoglucemiantes/farmacología , Sulfonamidas/farmacología , Compuestos de Sulfonilurea/farmacología , Animales , Simulación por Computador , Diabetes Mellitus Experimental/fisiopatología , Dipeptidil Peptidasa 4/efectos de los fármacos , Dipeptidil Peptidasa 4/metabolismo , Inhibidores de la Dipeptidil-Peptidasa IV/química , Inhibidores de la Dipeptidil-Peptidasa IV/farmacología , Femenino , Hipoglucemiantes/química , Insulina/metabolismo , Simulación del Acoplamiento Molecular , Ratas , Ratas Wistar , Estreptozocina , Sulfonamidas/química , Compuestos de Sulfonilurea/química
3.
Diabetes Res Clin Pract ; 97(1): 105-11, 2012 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-22410395

RESUMEN

The incretin based therapies are an emerging class of antidiabetic drugs, with two categories: one is glucagone like peptide-1 (GLP-1) agonists and the other one is dipeptidyl peptidase (CD26; DPP-IV) inhibitors. However, in the DPP-IV inhibitors category only few compounds are commercially available and also have some undesirable effects. Therefore, in the present work we tried to explore a naturally occurring compound naringin for its potential DPP-IV inhibition and antidiabetic potential. It is noteworthy that this compound is abundantly present in orange peel and thus may provide cost effective treatment for diabetes, especially type 2 diabetes mellitus. In the present study, we have conducted virtual docking study and observed tight binding of naringin, as shown by higher negative values of H bond lengths, while in vitro DPP-IV inhibition assay has also shown better inhibition by naringin. In vivo study, in response to 10 days administration of 40 mg/kg of naringin twice daily to Wistar albino rats, inhibited the serum levels of DPP-IV activity, random glucose concentration with concomitant increase in insulin levels. All the comparisons were made with the standard commercially available drug sitagliptin.


Asunto(s)
Diabetes Mellitus Experimental/tratamiento farmacológico , Diabetes Mellitus/tratamiento farmacológico , Inhibidores de la Dipeptidil-Peptidasa IV/farmacología , Flavanonas/farmacología , Hipoglucemiantes/farmacología , Páncreas/efectos de los fármacos , Animales , Glucemia/efectos de los fármacos , Glucemia/metabolismo , Simulación por Computador , Diabetes Mellitus/enzimología , Diabetes Mellitus Experimental/enzimología , Inhibidores de la Dipeptidil-Peptidasa IV/administración & dosificación , Esquema de Medicación , Femenino , Flavanonas/administración & dosificación , Péptido 1 Similar al Glucagón/agonistas , Humanos , Hipoglucemiantes/administración & dosificación , Técnicas In Vitro , Insulina/metabolismo , Peroxidación de Lípido , Masculino , Páncreas/enzimología , Ratas , Ratas Wistar
4.
Bioinformation ; 8(4): 185-8, 2012.
Artículo en Inglés | MEDLINE | ID: mdl-22419838

RESUMEN

Salmonella enteric serovar Typhi Ty2 is a human specific pathogen and an etiological agent for typhoid fever. Most of Salmonella serotypes produce glycogen which has a comparatively minor role in virulence and colonization, but has a more significant role in survival. Enzymes present in glycolytic pathway of bacteria help bacteria to survive by activating other factors inside host. Numerous pathogenic bacteria species intervene with the plasminogen system, and this plasminogen-enolase association may play a critical role in the virulence of S. Typhi by causing direct damage to the host cell extracellular matrix, possibly by enzymic degradation of extracellular matrix proteins or other protein constituents. In this study, molecular modelling of enolase of Salmonella has been accomplished in silico by comparative modelling; we have then analyzed Human alpha enolase which is a homodimer and serves on epithelial cells with our model. Both Structures were docked by D-tartronate semialdehyde phosphate (TSP) and 3-aminoenolpyruvate phosphate (AEP) enolase inhibitors. Our study shows that salmonella enolase and human enolase have different active sites in their structure. This will help in development of new ligands, more suitable for inhibiting bacterial survival inside host as vaccines for typhoid fever are not fully protective. The study also confirmed that enolase Salmonella and Human Plasminogen suggested direct physical interaction between both of them as the activation loop of plasminogen residues showed conformational changes similar to the tissue type plasminogen activator. Various computational biology tools were used for our present study such as Modeller, Molegro Virtual Docker, Grommacs.

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