Binding of folic acid induces specific self-aggregation of lactoferrin: thermodynamic characterization

Detalhes bibliográficos
Autor(a) principal: Tavares, Guilherme M.
Data de Publicação: 2015
Outros Autores: Croguennec, Thomas, Le, Sébastien, Lerideau, Olivia, Hamon, Pascaline, Carvalho, Antônio F., Bouhallab, Saïd
Tipo de documento: Artigo
Idioma: eng
Título da fonte: LOCUS Repositório Institucional da UFV
Texto Completo: https://pubs.acs.org/doi/10.1021/acs.langmuir.5b02299
http://www.locus.ufv.br/handle/123456789/19077
Resumo: In the study presented here, we investigated the interaction at pH 5.5 between folic acid (FA) and lactoferrin (LF), a positively charged protein. We found a binding constant Ka of 10(5) M(-1) and a high stoichiometry of 10 mol of FA/mol of LF. The size and charge of the complexes formed evolved during titration experiments. Increasing the ionic strength to 50 mM completely abolished the isothermal titration calorimetry (ITC) signal, suggesting the predominance of electrostatic interactions in the exothermic binding obtained. We developed a theoretical model that explains the complex triphasic ITC profile. Our results revealed a two-step mechanism: FA/LF interaction followed by self-association of the complexes thus formed. We suggest that 10 FA molecules bind to LF to form saturated reactive complexes (FA10/LF) that further self-associate into aggregates with a finite size of around 15 nm. There is thus a critical saturation degree of the protein, above which the self-association can take place. We present here the first results that provide comprehensive details of the thermodynamics of FA/LF complexation-association. Given the high stoichiometry, allowing a load of 55 mg of FA/g of LF, we suggest that FA/LF aggregates would be an effective vehicle for FA in fortified drinks.
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spelling Binding of folic acid induces specific self-aggregation of lactoferrin: thermodynamic characterizationFolic acidLactoferrinThermodynamic characterizationIn the study presented here, we investigated the interaction at pH 5.5 between folic acid (FA) and lactoferrin (LF), a positively charged protein. We found a binding constant Ka of 10(5) M(-1) and a high stoichiometry of 10 mol of FA/mol of LF. The size and charge of the complexes formed evolved during titration experiments. Increasing the ionic strength to 50 mM completely abolished the isothermal titration calorimetry (ITC) signal, suggesting the predominance of electrostatic interactions in the exothermic binding obtained. We developed a theoretical model that explains the complex triphasic ITC profile. Our results revealed a two-step mechanism: FA/LF interaction followed by self-association of the complexes thus formed. We suggest that 10 FA molecules bind to LF to form saturated reactive complexes (FA10/LF) that further self-associate into aggregates with a finite size of around 15 nm. There is thus a critical saturation degree of the protein, above which the self-association can take place. We present here the first results that provide comprehensive details of the thermodynamics of FA/LF complexation-association. Given the high stoichiometry, allowing a load of 55 mg of FA/g of LF, we suggest that FA/LF aggregates would be an effective vehicle for FA in fortified drinks.Langmuir2018-04-24T14:09:58Z2018-04-24T14:09:58Z2015-10-21info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlepdfapplication/pdf1520-5827https://pubs.acs.org/doi/10.1021/acs.langmuir.5b02299http://www.locus.ufv.br/handle/123456789/19077engv. 31, n. 45, p. 12481-12488, oct. 2015American Chemical Societyinfo:eu-repo/semantics/openAccessTavares, Guilherme M.Croguennec, ThomasLe, SébastienLerideau, OliviaHamon, PascalineCarvalho, Antônio F.Bouhallab, Saïdreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFV2024-07-12T07:08:06Zoai:locus.ufv.br:123456789/19077Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452024-07-12T07:08:06LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false
dc.title.none.fl_str_mv Binding of folic acid induces specific self-aggregation of lactoferrin: thermodynamic characterization
title Binding of folic acid induces specific self-aggregation of lactoferrin: thermodynamic characterization
spellingShingle Binding of folic acid induces specific self-aggregation of lactoferrin: thermodynamic characterization
Tavares, Guilherme M.
Folic acid
Lactoferrin
Thermodynamic characterization
title_short Binding of folic acid induces specific self-aggregation of lactoferrin: thermodynamic characterization
title_full Binding of folic acid induces specific self-aggregation of lactoferrin: thermodynamic characterization
title_fullStr Binding of folic acid induces specific self-aggregation of lactoferrin: thermodynamic characterization
title_full_unstemmed Binding of folic acid induces specific self-aggregation of lactoferrin: thermodynamic characterization
title_sort Binding of folic acid induces specific self-aggregation of lactoferrin: thermodynamic characterization
author Tavares, Guilherme M.
author_facet Tavares, Guilherme M.
Croguennec, Thomas
Le, Sébastien
Lerideau, Olivia
Hamon, Pascaline
Carvalho, Antônio F.
Bouhallab, Saïd
author_role author
author2 Croguennec, Thomas
Le, Sébastien
Lerideau, Olivia
Hamon, Pascaline
Carvalho, Antônio F.
Bouhallab, Saïd
author2_role author
author
author
author
author
author
dc.contributor.author.fl_str_mv Tavares, Guilherme M.
Croguennec, Thomas
Le, Sébastien
Lerideau, Olivia
Hamon, Pascaline
Carvalho, Antônio F.
Bouhallab, Saïd
dc.subject.por.fl_str_mv Folic acid
Lactoferrin
Thermodynamic characterization
topic Folic acid
Lactoferrin
Thermodynamic characterization
description In the study presented here, we investigated the interaction at pH 5.5 between folic acid (FA) and lactoferrin (LF), a positively charged protein. We found a binding constant Ka of 10(5) M(-1) and a high stoichiometry of 10 mol of FA/mol of LF. The size and charge of the complexes formed evolved during titration experiments. Increasing the ionic strength to 50 mM completely abolished the isothermal titration calorimetry (ITC) signal, suggesting the predominance of electrostatic interactions in the exothermic binding obtained. We developed a theoretical model that explains the complex triphasic ITC profile. Our results revealed a two-step mechanism: FA/LF interaction followed by self-association of the complexes thus formed. We suggest that 10 FA molecules bind to LF to form saturated reactive complexes (FA10/LF) that further self-associate into aggregates with a finite size of around 15 nm. There is thus a critical saturation degree of the protein, above which the self-association can take place. We present here the first results that provide comprehensive details of the thermodynamics of FA/LF complexation-association. Given the high stoichiometry, allowing a load of 55 mg of FA/g of LF, we suggest that FA/LF aggregates would be an effective vehicle for FA in fortified drinks.
publishDate 2015
dc.date.none.fl_str_mv 2015-10-21
2018-04-24T14:09:58Z
2018-04-24T14:09:58Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv 1520-5827
https://pubs.acs.org/doi/10.1021/acs.langmuir.5b02299
http://www.locus.ufv.br/handle/123456789/19077
identifier_str_mv 1520-5827
url https://pubs.acs.org/doi/10.1021/acs.langmuir.5b02299
http://www.locus.ufv.br/handle/123456789/19077
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv v. 31, n. 45, p. 12481-12488, oct. 2015
dc.rights.driver.fl_str_mv American Chemical Society
info:eu-repo/semantics/openAccess
rights_invalid_str_mv American Chemical Society
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv pdf
application/pdf
dc.publisher.none.fl_str_mv Langmuir
publisher.none.fl_str_mv Langmuir
dc.source.none.fl_str_mv reponame:LOCUS Repositório Institucional da UFV
instname:Universidade Federal de Viçosa (UFV)
instacron:UFV
instname_str Universidade Federal de Viçosa (UFV)
instacron_str UFV
institution UFV
reponame_str LOCUS Repositório Institucional da UFV
collection LOCUS Repositório Institucional da UFV
repository.name.fl_str_mv LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)
repository.mail.fl_str_mv fabiojreis@ufv.br
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