Search

Your search keyword '"D. Gerbino"' showing total 4 results
Start Over Author "D. Gerbino"
4 results on '"D. Gerbino"'

1. Effects of hydroxy-xanthones on dipalmitoylphosphatidylcholine lipid bilayers: A theoretical and experimental study

Author

Marcela A. Morini, Flavia Edith Buffo, L. M. Alarcón, Viviana Isabel Pedroni, María Belén Sierra, and D. Gerbino

Subjects
Dppc liposomes, 1,2-Dipalmitoylphosphatidylcholine, Chemical Phenomena, Xanthones, MOLECULAR DYNAMICS SIMULATIONS, Lipid Bilayers, Molecular Dynamics Simulation, 01 natural sciences, Biochemistry, chemistry.chemical_compound, Molecular dynamics, Computational chemistry, 0103 physical sciences, Xanthone, Zeta potential, Organic chemistry, DPPC LIPOSOME, Lipid bilayer, Molecular Biology, FLUIDITY, Liposome, 010304 chemical physics, XANTHONES, 010405 organic chemistry, Bilayer, Otras Ciencias Químicas, Organic Chemistry, Ciencias Químicas, Temperature, Cell Biology, 0104 chemical sciences, chemistry, Dipalmitoylphosphatidylcholine, lipids (amino acids, peptides, and proteins), ZETA POTENTIAL, CIENCIAS NATURALES Y EXACTAS
Abstract

Xanthones and derivatives are natural active compounds whose interest has been increased due to its several pharmacological effects. In this work, effects of hydroxy-xanthones on the physicochemical properties of dipalmitoylphosphatidylcholine (DPPC) liposomes have been investigated in terms of lipid bilayer fluidity, by means of molecular dynamics simulations and temperature dependence of zeta potential studies. Experimental results predict, in good agreement with simulations, that xanthones are able to be incorporated into DPPC liposomes with certain localization, fluidizing the bilayer. Both effects, localization and fluidity were found to be dependent of the number of hydroxilic substituents of the xanthone and the lipid phase state. Fil: Sierra, Maria Belen. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; Argentina Fil: Alarcon, Laureano Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; Argentina Fil: Gerbino, Darío César. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; Argentina Fil: Pedroni, Viviana Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; Argentina Fil: Buffo, Flavia Edith. Universidad Nacional del Sur. Departamento de Matemática; Argentina Fil: Morini, Marcela Ana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; Argentina

Published
2016

2. Dynamic Analysis of Backbone-Hydrogen-Bond Propensity for Protein Binding and Drug Design

Author

C Menéndez, S Accordino, J Rodriguez, D Gerbino, and G Appignanesi

Subjects
chemistry.chemical_classification, Molecular dynamics, Protein structure, Chemistry, Hydrogen bond, Protein dynamics, Protein Data Bank (RCSB PDB), Biophysics, Non-covalent interactions, Plasma protein binding, computer.file_format, Protein Data Bank, computer
Abstract

The three-dimensional shape of a protein recorded in the Protein Data Bank (PDB) provides valuable information regarding its structure and stability. However, such a static picture might be veiling relevant information regarding protein dynamics and function. In fact, backbone hydrogen bonds (BHBs), as main determinants of protein structure, constitute context-dependent noncovalent interactions. These interactions face different environments along the protein chain, particularly at protein binding sites which might present different hydration properties from that of other regions of the protein surface. Here we characterize the hydration and hydrophobicity of protein binding sites by molecular dynamics (MD) simulations, focusing particularly on their BHBs. We also carry out a time-averaged contact matrix study to reveal the existence of BHBs whose net persistence in time differs markedly from their corresponding PDB-reported state. Such interactions where the PDB failsINQUISUR-UNS-CONICET and Departamento de Quimica, Universidad Nacional del Sur, Avenida Alem 1253, 8000-Bahia Blanca, Argentina.

Published
2016
Full Text
View/download PDF

3. A New Antagonist of Caenorhabditis elegans Glutamate-Activated Chloride Channels With Anthelmintic Activity.

Author

Castro MJ, Turani O, Faraoni MB, Gerbino D, and Bouzat C

Abstract

Nematode parasitosis causes significant mortality and morbidity in humans and considerable losses in livestock and domestic animals. The acquisition of resistance to current anthelmintic drugs has prompted the search for new compounds for which the free-living nematode Caenorhabditis elegans has emerged as a valuable platform. We have previously synthetized a small library of oxygenated tricyclic compounds and determined that dibenzo[ b,e ]oxepin-11(6H)-one (doxepinone) inhibits C. elegans motility. Because doxepinone shows potential anthelmintic activity, we explored its behavioral effects and deciphered its target site and mechanism of action on C. elegans. Doxepinone reduces swimming rate, induces paralysis, and decreases the rate of pharyngeal pumping required for feeding, indicating a marked anthelmintic activity. To identify the main drug targets, we performed an in vivo screening of selected strains carrying mutations in Cys-loop receptors involved in worm locomotion for determining resistance to doxepinone effects. A mutant strain that lacks subunit genes of the invertebrate glutamate-gated chloride channels (GluCl), which are targets of the widely used antiparasitic ivermectin (IVM), is resistant to doxepinone effects. To unravel the molecular mechanism, we measured whole-cell currents from GluClα1/β receptors expressed in mammalian cells. Glutamate elicits macroscopic currents whereas no responses are elicited by doxepinone, indicating that it is not an agonist of GluCls. Preincubation of the cell with doxepinone produces a statistically significant decrease of the decay time constant and net charge of glutamate-elicited currents, indicating that it inhibits GluCls, which contrasts to IVM molecular actions. Thus, we identify doxepinone as an attractive scaffold with promising anthelmintic activity and propose the inhibition of GluCls as a potential anthelmintic mechanism of action., (Copyright © 2020 Castro, Turani, Faraoni, Gerbino and Bouzat.)

Published
2020
Full Text
View/download PDF

4. Effects of hydroxy-xanthones on dipalmitoylphosphatidylcholine lipid bilayers: A theoretical and experimental study.

Author

Sierra MB, Alarcón L, Gerbino D, Pedroni VI, Buffo FE, and Morini MA

Subjects
Chemical Phenomena drug effects, Temperature, 1,2-Dipalmitoylphosphatidylcholine chemistry, Lipid Bilayers chemistry, Molecular Dynamics Simulation, Xanthones chemistry, Xanthones pharmacology
Abstract

Xanthones and derivatives are natural active compounds whose interest has been increased due to its several pharmacological effects. In this work, effects of hydroxy-xanthones on the physicochemical properties of dipalmitoylphosphatidylcholine (DPPC) liposomes have been investigated in terms of lipid bilayer fluidity, by means of molecular dynamics simulations and temperature dependence of zeta potential studies. Experimental results predict, in good agreement with simulations, that xanthones are able to be incorporated into DPPC liposomes with certain localization, fluidizing the bilayer. Both effects, localization and fluidity were found to be dependent of the number of hydroxilic substituents of the xanthone and the lipid phase state., (Copyright © 2017 Elsevier B.V. All rights reserved.)

Published
2017
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results