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Relevance of the protein macrodipole in the membrane-binding process. Interactions of fatty-acid binding proteins with cationic lipid membranes

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      Abstract

      The fatty acid-binding proteins L-BABP and Rep1-NCXSQ bind to anionic lipid membranes by electrostatic interactions. According to Molecular Dynamics (MD) simulations, the interaction of the protein macrodipole with the membrane electric field is a driving force for protein binding and orientation in the interface. To further explore this hypothesis, we studied the interactions of these proteins with cationic lipid membranes. As in the case of anionic lipid membranes, we found that both proteins, carrying a negative as well as a positive net charge, were bound to the positively charged membrane. Their major axis, those connecting the bottom of the β-barrel with the α-helix portal domain, were rotated about 180 degrees as compared with their orientations in the anionic lipid membranes. Fourier transform infrared (FTIR) spectroscopy of the proteins showed that the positively charged membranes were also able to induce conformational changes with a reduction of the β-strand proportion and an increase in α-helix secondary structure. Fatty acid-binding proteins (FABPs) are involved in several cell processes, such as maintaining lipid homeostasis in cells. They transport hydrophobic molecules in aqueous medium and deliver them into lipid membranes. Therefore, the interfacial orientation and conformation, both shown herein to be electrostatically determined, have a strong correlation with the specific mechanism by which each particular FABP exerts its biological function.

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      Most cited references 52

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      Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features.

       C. Sander,  W Kabsch (1983)
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        VMD: visual molecular dynamics.

        VMD is a molecular graphics program designed for the display and analysis of molecular assemblies, in particular biopolymers such as proteins and nucleic acids. VMD can simultaneously display any number of structures using a wide variety of rendering styles and coloring methods. Molecules are displayed as one or more "representations," in which each representation embodies a particular rendering method and coloring scheme for a selected subset of atoms. The atoms displayed in each representation are chosen using an extensive atom selection syntax, which includes Boolean operators and regular expressions. VMD provides a complete graphical user interface for program control, as well as a text interface using the Tcl embeddable parser to allow for complex scripts with variable substitution, control loops, and function calls. Full session logging is supported, which produces a VMD command script for later playback. High-resolution raster images of displayed molecules may be produced by generating input scripts for use by a number of photorealistic image-rendering applications. VMD has also been expressly designed with the ability to animate molecular dynamics (MD) simulation trajectories, imported either from files or from a direct connection to a running MD simulation. VMD is the visualization component of MDScope, a set of tools for interactive problem solving in structural biology, which also includes the parallel MD program NAMD, and the MDCOMM software used to connect the visualization and simulation programs. VMD is written in C++, using an object-oriented design; the program, including source code and extensive documentation, is freely available via anonymous ftp and through the World Wide Web.
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          Electrostatics of nanosystems: application to microtubules and the ribosome.

          Evaluation of the electrostatic properties of biomolecules has become a standard practice in molecular biophysics. Foremost among the models used to elucidate the electrostatic potential is the Poisson-Boltzmann equation; however, existing methods for solving this equation have limited the scope of accurate electrostatic calculations to relatively small biomolecular systems. Here we present the application of numerical methods to enable the trivially parallel solution of the Poisson-Boltzmann equation for supramolecular structures that are orders of magnitude larger in size. As a demonstration of this methodology, electrostatic potentials have been calculated for large microtubule and ribosome structures. The results point to the likely role of electrostatics in a variety of activities of these structures.
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            Author and article information

            Affiliations
            [1 ] Universidad Nacional de Córdoba, Facultad de Ciencias Químicas, Departamento de Química Biológica “Ranwel Caputto”, Córdoba, Argentina
            [2 ] CONICET, Universidad Nacional de Córdoba, Centro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC), Córdoba, Argentina
            [3 ] Universidad Nacional de Córdoba, Facultad de Ciencias Químicas, Departamento de Química Teórica y Computacional, Córdoba, Argentina
            [4 ] CONICET, Universidad Nacional de Córdoba. Instituto de Investigaciones en Fisicoquímica de Córdoba (INFIQC), Córdoba, Argentina
            University of Waterloo, CANADA
            Author notes

            Competing Interests: The authors have declared that no competing interests exist.

            [¤]

            Current address: CONICET, Facultad de Ciencias Exactas y Naturales, Universidad Nacional de Cuyo, Mendoza, Argentina.

            Contributors
            Role: Conceptualization, Role: Data curation, Role: Formal analysis, Role: Writing – original draft
            Role: Conceptualization
            ORCID: http://orcid.org/0000-0002-7389-0038, Role: Conceptualization, Role: Funding acquisition, Role: Project administration, Role: Supervision, Role: Writing – review & editing
            Role: Editor
            Journal
            PLoS One
            PLoS ONE
            plos
            plosone
            PLoS ONE
            Public Library of Science (San Francisco, CA USA )
            1932-6203
            8 March 2018
            2018
            : 13
            : 3
            29518146
            5843346
            10.1371/journal.pone.0194154
            PONE-D-17-33567
            (Editor)
            © 2018 Galassi et al

            This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

            Counts
            Figures: 8, Tables: 2, Pages: 15
            Product
            Funding
            Funded by: Consejo Nacional de Investigaciones Científicas y Técnicas (AR)
            Award ID: PIP 2013-2015
            Funded by: funder-id http://dx.doi.org/10.13039/501100006668, Fondo para la Investigación Científica y Tecnológica;
            Award ID: PICT 2015-1612
            This work was supported by Consejo Nacional de Investigaciones Científicas y Técnicas (AR), PIP 2013-2015; Fondo para la Investigación Científica y Tecnológica, PICT 2015-1612; and Secretaría de Ciencia y Técnica UNC.
            Categories
            Research Article
            Biology and Life Sciences
            Biochemistry
            Lipids
            Biology and Life Sciences
            Biochemistry
            Biochemical Simulations
            Biology and Life Sciences
            Computational Biology
            Biochemical Simulations
            Biology and Life Sciences
            Biochemistry
            Proteins
            Protein Interactions
            Biology and Life Sciences
            Cell Biology
            Cellular Structures and Organelles
            Cell Membranes
            Membrane Proteins
            Peripheral Membrane Proteins
            Research and Analysis Methods
            Bioassays and Physiological Analysis
            Electrophysiological Techniques
            Membrane Electrophysiology
            Physical Sciences
            Physics
            Electricity
            Electric Field
            Physical Sciences
            Physics
            Electricity
            Electrostatics
            Physical Sciences
            Chemistry
            Physical Chemistry
            Chemical Bonding
            Electrostatic Bonding
            Custom metadata
            All relevant data are within the paper and the Supporting Information files.

            Uncategorized

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