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2 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
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