Deen Dayal Upadhyay Gorakhpur University

About: Deen Dayal Upadhyay Gorakhpur University is a education organization based out in Gorakhpur, Uttar Pradesh, India. It is known for research contribution in the topics: Thermal decomposition & Lymnaea acuminata. The organization has 1032 authors who have published 1591 publications receiving 21734 citations. The organization is also known as: Gorakhpur University.

Antidiabetic potential of plant natural products: A review

Abstract: The present review explains the use of natural plant products for therapeutics of diabetes. It is a serious metabolic disorder that imposes multiple effects on human health. Although diabetes is curable, an erratic lifestyle always make panic and causes disease severity if proper medication is not being made available. Several ethnomedicines have been used by local people in form of crude extracts prepared from flowers, fruits, and roots of endemic plant species for cure of diabetes. There is a common usage of herbal parts for preparation of concoctions, syrups, vegetables, juices, green tea, from leaves, and roots for therapeutic purposes. This article explains antidiabetic effects of various plant secondary metabolites such as anthraquinones, flavonoids, secoiridoids, iridoids, flavanones, biophenols, triterpenes, benzoic acid derivatives, isochromans, and phytosterols. Daily meals containing good nutraceuticals such as protein and fiber can replace carbohydrate food that is a main source of glucose. Mainly, herbal foods rich in flavanols and polyphenols show hypoglycemic effects and can be used in the prevention of diabetes-induced vascular dysfunctions. Antidiabetic plant natural products restore insulin level and increase utilization of external glucose. Herbal dietary supplementation having diverse antioxidants, fibers, minerals, and antiglycants show inhibitory activity against α-amylase and α-glycosidase can easily control carbohydrate metabolism in humans. No doubt plant origin natural products can be used as alternative medicine for treatment of diabetes, but they must need proper composition and formulation before being used.

Computational and In Vitro Investigation of (-)-Epicatechin and Proanthocyanidin B2 as Inhibitors of Human Matrix Metalloproteinase 1.

Abstract: Matrix metalloproteinases 1 (MMP-1) energetically triggers the enzymatic proteolysis of extracellular matrix collagenase (ECM), resulting in progressive skin aging. Natural flavonoids are well known for their antioxidant properties and have been evaluated for inhibition of matrix metalloproteins in human. Recently, (-)-epicatechin and proanthocyanidin B2 were reported as essential flavanols from various natural reservoirs as potential anti-inflammatory and free radical scavengers. However, their molecular interactions and inhibitory potential against MMP-1 are not yet well studied. In this study, sequential absorption, distribution, metabolism, and excretion (ADME) profiling, quantum mechanics calculations, and molecular docking simulations by extra precision Glide protocol predicted the drug-likeness of (-)-epicatechin (-7.862 kcal/mol) and proanthocyanidin B2 (-8.145 kcal/mol) with the least reactivity and substantial binding affinity in the catalytic pocket of human MMP-1 by comparison to reference bioactive compound epigallocatechin gallate (-6.488 kcal/mol). These flavanols in docked complexes with MMP-1 were further studied by 500 ns molecular dynamics simulations that revealed substantial stability and intermolecular interactions, viz. hydrogen and ionic interactions, with essential residues, i.e., His218, Glu219, His222, and His228, in the active pocket of MMP-1. In addition, binding free energy calculations using the Molecular Mechanics Generalized Born Surface Area (MM/GBSA) method suggested the significant role of Coulomb interactions and van der Waals forces in the stability of respective docked MMP-1-flavonol complexes by comparison to MMP-1-epigallocatechin gallate; these observations were further supported by MMP-1 inhibition assay using zymography. Altogether with computational and MMP-1-zymography results, our findings support (-)-epicatechin as a comparatively strong inhibitor of human MMP-1 with considerable drug-likeness against proanthocyanidin B2 in reference to epigallocatechin gallate.

In vitro PHYTOTHERAPY OF VECTOR SNAILS BY BINARY COMBINATIONS OF LARVICIDAL ACTIVE COMPONENTS IN EFFECTIVE CONTROL OF FASCIOLIASIS

Abstract: RESUMO A infeccao alimentar pelo trematoide da fascioliase e uma dentre os mais comuns problemas de saude publica mundiais, causando grande prejuizo economico para a humanidade. Controle da populacao de caramujos abaixo de determinado nivel e um dos metodos no campo mais importantes para a reducao da incidencia da fascioliase. O ciclo de vida do parasita pode ser interrompido pela morte do caramujo ou da larva redia e cercaria da Fasciola dentro da Lymnaea acuminata. Foi testada a toxicidade in vitro das diferentes combinacoes binarias (relacao 1:1) entre os varios componentes larvicidas ativos da planta tais como citral, acido ferulico, umbeliferone, azadiractina, e alicina contra a Fasciola redia e a cercaria. A mortalidade das larvas foi observada apos duas, quatro, seis e oito horas de tratamento. A condicao in vitro azadiractina + alicina (relacao 1:1) foi altamente toxica contra redia e cercaria (8h LC50 0,006 e 0,005 mg/L). Toxicidade do citral + acido ferulico foi a mais baixa contra redia e larvas de cercaria.

PURIFICATION AND BIOCHEMICAL CHARACTERIZATION OF IONICALLY UNBOUND POLYPHENOL OXIDASE FROM Musa paradisiaca LEAF

Abstract: An ionically unbound and thermostable polyphenol oxidase (PPO) was extracted from the leaf of Musa paradisiaca. The enzyme was purified 2.54-fold with a total yield of 9.5% by ammonium sulfate precipitation followed by Sephadex G-100 gel filtration chromatography. The purified enzyme exhibited a clear single band on native polyacrylamide gel electrophoresis (PAGE) and sodium dodecyl sulfate (SDS) PAGE. It was found to be monomeric protein with molecular mass of about 40 kD. The zymographic study using crude extract as enzyme source showed a very clear band around 40 kD and a faint band at around 15 kD, which might be isozymes. The enzyme was optimally active at pH 7.0 and 50°C temperature. The enzyme was active in wide range of pH (4.0-9.0) and temperature (30-90°C). From the thermal inactivation studies in the range 60-75°C, the half-life (t(1/2)) values of the enzyme ranged from 17 to 77 min. The inactivation energy (Ea) value of PPO was estimated to be 91.3 kJ mol(-1). It showed higher specificity with catechol (K(m) = 8 mM) as compared to 4-methylcatechol (K(m) = 10 mM). Among metal ions and reagents tested, Cu(2+), Fe(2+), Hg(2+), Mn(2+), Ni(2+), protocatechuic acid, and ferrulic acid enhanced the enzyme activity, while K(+), Na(+), Co(2+), kojic acid, ascorbic acid, ethylenediamine tetraacetic acid (EDTA), sodium azide, β-mercaptoethanol, and L-cysteine inhibited the activity of the enzyme.