Cooperativity in binding processes: New insights from phenomenological modeling

Cooperative binding is one of the most interesting and not fully understood phenomena involved in control and regulation of biological processes. Here we analyze the simplest phenomenological model that can account for cooperativity (i.e. ligand binding to a macromolecule with two binding sites) by...

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Detalles Bibliográficos
Autores principales: Cattoni, Diego I., Chara, Osvaldo, Kaufman, Sergio B., González Flecha, F. Luis
Formato: Articulo
Lenguaje:Inglés
Publicado: 2015
Materias:
Ciencias Exactas
Cooperative binding
Biological processes
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/86415
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-86415
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Exactas
Cooperative binding
Biological processes
spellingShingle Ciencias Exactas
Cooperative binding
Biological processes
Cattoni, Diego I.
Chara, Osvaldo
Kaufman, Sergio B.
González Flecha, F. Luis
Cooperativity in binding processes: New insights from phenomenological modeling
topic_facet Ciencias Exactas
Cooperative binding
Biological processes
description Cooperative binding is one of the most interesting and not fully understood phenomena involved in control and regulation of biological processes. Here we analyze the simplest phenomenological model that can account for cooperativity (i.e. ligand binding to a macromolecule with two binding sites) by generating equilibrium binding isotherms from deterministically simulated binding time courses. We show that the Hill coefficients determined for cooperative binding, provide a good measure of the Gibbs free energy of interaction among binding sites, and that their values are independent of the free energy of association for empty sites. We also conclude that although negative cooperativity and different classes of binding sites cannot be distinguished at equilibrium, they can be kinetically differentiated. This feature highlights the usefulness of pre-equilibrium time-resolved strategies to explore binding models as a key complement of equilibrium experiments. Furthermore, our analysis shows that under conditions of strong negative cooperativity, the existence of some binding sites can be overlooked, and experiments at very high ligand concentrations can be a valuable tool to unmask such sites.
format Articulo
Articulo
author Cattoni, Diego I.
Chara, Osvaldo
Kaufman, Sergio B.
González Flecha, F. Luis
author_facet Cattoni, Diego I.
Chara, Osvaldo
Kaufman, Sergio B.
González Flecha, F. Luis
author_sort Cattoni, Diego I.
title Cooperativity in binding processes: New insights from phenomenological modeling
title_short Cooperativity in binding processes: New insights from phenomenological modeling
title_full Cooperativity in binding processes: New insights from phenomenological modeling
title_fullStr Cooperativity in binding processes: New insights from phenomenological modeling
title_full_unstemmed Cooperativity in binding processes: New insights from phenomenological modeling
title_sort cooperativity in binding processes: new insights from phenomenological modeling
publishDate 2015
url http://sedici.unlp.edu.ar/handle/10915/86415
work_keys_str_mv AT cattonidiegoi cooperativityinbindingprocessesnewinsightsfromphenomenologicalmodeling
AT charaosvaldo cooperativityinbindingprocessesnewinsightsfromphenomenologicalmodeling
AT kaufmansergiob cooperativityinbindingprocessesnewinsightsfromphenomenologicalmodeling
AT gonzalezflechafluis cooperativityinbindingprocessesnewinsightsfromphenomenologicalmodeling
bdutipo_str Repositorios
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