Computational predictions on the interactions of parabens with a dipalmitoyl phosphatidylcholine lipid bilayer and the human serum albumin protein

Autores
Masone, Diego Fernando; Félix Rubio Dalmau
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Parabens are esters of para-hydroxybenzoic acid extensively used as preservatives in cosmetics and pharmaceutics. In the recent years their safe use has been questioned, mainly due to their estrogenic activity, their concentration in breast cancer tissues and their endocrine disrupting consequences on the reproductive system. In this study, the interaction of five forms of paraben ligands (namely methyl, ethyl, propyl, butyl and heptyl) with a model dipalmitoylphosphatidylcholine bilayer and the human serum albumin transport protein, was assessed using extensive atomistic molecular dynamics simulations. Free energy profiles for the insertion of each ligand into the lipid bilayer were computed along an appropriate reaction coordinate. Protein-ligand interactions were evaluated through a combination of an efficient sampling of the protein-ligand hydrogen bond network and the full system side chains, together with an all-atom force field. Simulation results show that among the paraben ligands studied, methyl, propyl and butyl parabens penetrate more easily the bilayer and show higher binding affinity to human serum albumin in terms of their hydrogen bonding network, supporting the experimental hypotheses of their potential risk to human health.
Fil: Masone, Diego Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Cienicas Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
Fil: Félix Rubio Dalmau. Barcelona Supercomputing Center; España
Materia
Parabens
Hsa
Molecular Dynamics
Docking
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/48748
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Computational predictions on the interactions of parabens with a dipalmitoyl phosphatidylcholine lipid bilayer and the human serum albumin proteinMasone, Diego FernandoFélix Rubio DalmauParabensHsaMolecular DynamicsDockinghttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Parabens are esters of para-hydroxybenzoic acid extensively used as preservatives in cosmetics and pharmaceutics. In the recent years their safe use has been questioned, mainly due to their estrogenic activity, their concentration in breast cancer tissues and their endocrine disrupting consequences on the reproductive system. In this study, the interaction of five forms of paraben ligands (namely methyl, ethyl, propyl, butyl and heptyl) with a model dipalmitoylphosphatidylcholine bilayer and the human serum albumin transport protein, was assessed using extensive atomistic molecular dynamics simulations. Free energy profiles for the insertion of each ligand into the lipid bilayer were computed along an appropriate reaction coordinate. Protein-ligand interactions were evaluated through a combination of an efficient sampling of the protein-ligand hydrogen bond network and the full system side chains, together with an all-atom force field. Simulation results show that among the paraben ligands studied, methyl, propyl and butyl parabens penetrate more easily the bilayer and show higher binding affinity to human serum albumin in terms of their hydrogen bonding network, supporting the experimental hypotheses of their potential risk to human health.Fil: Masone, Diego Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Cienicas Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Félix Rubio Dalmau. Barcelona Supercomputing Center; EspañaOpen Access Text2016-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/48748Masone, Diego Fernando; Félix Rubio Dalmau; Computational predictions on the interactions of parabens with a dipalmitoyl phosphatidylcholine lipid bilayer and the human serum albumin protein; Open Access Text; Interdisciplinary Journal of Chemistry; 1; 9-2016; 20-272398-7537CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.oatext.com/Computational-predictions-on-the-interactions-of-parabens-with-a-dipalmitoylphosphatidylcholine-lipid-bilayer-and-the-human-serum-albumin-protein.phpinfo:eu-repo/semantics/altIdentifier/doi/10.15761/IJC.1000104info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:10:13Zoai:ri.conicet.gov.ar:11336/48748instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 15:10:13.682CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Computational predictions on the interactions of parabens with a dipalmitoyl phosphatidylcholine lipid bilayer and the human serum albumin protein
title Computational predictions on the interactions of parabens with a dipalmitoyl phosphatidylcholine lipid bilayer and the human serum albumin protein
spellingShingle Computational predictions on the interactions of parabens with a dipalmitoyl phosphatidylcholine lipid bilayer and the human serum albumin protein
Masone, Diego Fernando
Parabens
Hsa
Molecular Dynamics
Docking
title_short Computational predictions on the interactions of parabens with a dipalmitoyl phosphatidylcholine lipid bilayer and the human serum albumin protein
title_full Computational predictions on the interactions of parabens with a dipalmitoyl phosphatidylcholine lipid bilayer and the human serum albumin protein
title_fullStr Computational predictions on the interactions of parabens with a dipalmitoyl phosphatidylcholine lipid bilayer and the human serum albumin protein
title_full_unstemmed Computational predictions on the interactions of parabens with a dipalmitoyl phosphatidylcholine lipid bilayer and the human serum albumin protein
title_sort Computational predictions on the interactions of parabens with a dipalmitoyl phosphatidylcholine lipid bilayer and the human serum albumin protein
dc.creator.none.fl_str_mv Masone, Diego Fernando
Félix Rubio Dalmau
author Masone, Diego Fernando
author_facet Masone, Diego Fernando
Félix Rubio Dalmau
author_role author
author2 Félix Rubio Dalmau
author2_role author
dc.subject.none.fl_str_mv Parabens
Hsa
Molecular Dynamics
Docking
topic Parabens
Hsa
Molecular Dynamics
Docking
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Parabens are esters of para-hydroxybenzoic acid extensively used as preservatives in cosmetics and pharmaceutics. In the recent years their safe use has been questioned, mainly due to their estrogenic activity, their concentration in breast cancer tissues and their endocrine disrupting consequences on the reproductive system. In this study, the interaction of five forms of paraben ligands (namely methyl, ethyl, propyl, butyl and heptyl) with a model dipalmitoylphosphatidylcholine bilayer and the human serum albumin transport protein, was assessed using extensive atomistic molecular dynamics simulations. Free energy profiles for the insertion of each ligand into the lipid bilayer were computed along an appropriate reaction coordinate. Protein-ligand interactions were evaluated through a combination of an efficient sampling of the protein-ligand hydrogen bond network and the full system side chains, together with an all-atom force field. Simulation results show that among the paraben ligands studied, methyl, propyl and butyl parabens penetrate more easily the bilayer and show higher binding affinity to human serum albumin in terms of their hydrogen bonding network, supporting the experimental hypotheses of their potential risk to human health.
Fil: Masone, Diego Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Cienicas Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
Fil: Félix Rubio Dalmau. Barcelona Supercomputing Center; España
description Parabens are esters of para-hydroxybenzoic acid extensively used as preservatives in cosmetics and pharmaceutics. In the recent years their safe use has been questioned, mainly due to their estrogenic activity, their concentration in breast cancer tissues and their endocrine disrupting consequences on the reproductive system. In this study, the interaction of five forms of paraben ligands (namely methyl, ethyl, propyl, butyl and heptyl) with a model dipalmitoylphosphatidylcholine bilayer and the human serum albumin transport protein, was assessed using extensive atomistic molecular dynamics simulations. Free energy profiles for the insertion of each ligand into the lipid bilayer were computed along an appropriate reaction coordinate. Protein-ligand interactions were evaluated through a combination of an efficient sampling of the protein-ligand hydrogen bond network and the full system side chains, together with an all-atom force field. Simulation results show that among the paraben ligands studied, methyl, propyl and butyl parabens penetrate more easily the bilayer and show higher binding affinity to human serum albumin in terms of their hydrogen bonding network, supporting the experimental hypotheses of their potential risk to human health.
publishDate 2016
dc.date.none.fl_str_mv 2016-09
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/48748
Masone, Diego Fernando; Félix Rubio Dalmau; Computational predictions on the interactions of parabens with a dipalmitoyl phosphatidylcholine lipid bilayer and the human serum albumin protein; Open Access Text; Interdisciplinary Journal of Chemistry; 1; 9-2016; 20-27
2398-7537
CONICET Digital
CONICET
url http://hdl.handle.net/11336/48748
identifier_str_mv Masone, Diego Fernando; Félix Rubio Dalmau; Computational predictions on the interactions of parabens with a dipalmitoyl phosphatidylcholine lipid bilayer and the human serum albumin protein; Open Access Text; Interdisciplinary Journal of Chemistry; 1; 9-2016; 20-27
2398-7537
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.oatext.com/Computational-predictions-on-the-interactions-of-parabens-with-a-dipalmitoylphosphatidylcholine-lipid-bilayer-and-the-human-serum-albumin-protein.php
info:eu-repo/semantics/altIdentifier/doi/10.15761/IJC.1000104
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Open Access Text
publisher.none.fl_str_mv Open Access Text
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.22299

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