Insight into Molecular Interactions of Two Methyl Benzoate Derivatives with Bovine Serum Albumin

The nature and mechanisms of interaction between two selected methyl benzoate derivatives (methyl o-methoxy p-methylaminobenzoate–I and methyl o-hydroxy p-methylaminobenzoate–II) and mod...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Karolina Baranowska, Michał Mońka, Piotr Bojarski, Marek Józefowicz
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	inclusion complex bovine serum albumin tryptophan excited-state intramolecular proton transfer supramolecular interactions Biology (General) QH301-705.5 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/a53cd76ee3a8468f81b3ccb33a4e91a9
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:a53cd76ee3a8468f81b3ccb33a4e91a9
record_format	dspace
spelling	oai:doaj.org-article:a53cd76ee3a8468f81b3ccb33a4e91a92021-11-11T17:09:51ZInsight into Molecular Interactions of Two Methyl Benzoate Derivatives with Bovine Serum Albumin10.3390/ijms2221117051422-00671661-6596https://doaj.org/article/a53cd76ee3a8468f81b3ccb33a4e91a92021-10-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/21/11705https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067The nature and mechanisms of interaction between two selected methyl benzoate derivatives (methyl <i>o</i>-methoxy <i>p</i>-methylaminobenzoate–<b>I</b> and methyl <i>o</i>-hydroxy <i>p</i>-methylaminobenzoate–<b>II</b>) and model transport protein bovine serum albumin (BSA) was studied using steady-state and time-resolved spectroscopic techniques. In order to understand the role of Trp residue of BSA in the <b>I</b>-BSA and <b>II</b>-BSA interaction, the effect of free Trp amino acid on the both emission modes (LE–locally excited (<b>I</b> and <b>II</b>) and ESIPT–excited state intramolecular proton transfer (<b>II</b>)) was investigated as well. Experimental results show that the investigated interactions (with both BSA and Trp) are mostly conditioned by the ground and excited state complex formation processes. Both molecules form stable complexes with BSA and Trp (with 1:1 stoichiometry) in the ground and excited states. The binding constants were in the order of 10<sup>4</sup> M<sup>−1</sup>. The absorption- and fluorescence-titration experiments along with the time-resolved fluorescence measurements show that the binding of the <b>I</b> and <b>II</b> causes fluorescence quenching of BSA through the static mechanism, revealing a 1:1 interaction. The magnitude and the sign of the thermodynamic parameters, Δ<i>H</i>, Δ<i>S</i>, and Δ<i>G</i>, determined from van’t Hoff relationship, confirm the predominance of the hydrogen-bonding interactions for the binding phenomenon. To improve and complete knowledge of methyl benzoate derivative-protein interactions in relation to supramolecular solvation dynamics, the time-dependent fluorescence Stokes’ shifts, represented by the normalized spectral response function <i>c(t)</i>, was studied. Our studies reveal that the solvation dynamics that occurs in subpicosecond time scale in neat solvents of different polarities is slowed down significantly when the organic molecule is transferred to BSA cavity.Karolina BaranowskaMichał MońkaPiotr BojarskiMarek JózefowiczMDPI AGarticleinclusion complexbovine serum albumintryptophanexcited-state intramolecular proton transfersupramolecular interactionsBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 11705, p 11705 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	inclusion complex bovine serum albumin tryptophan excited-state intramolecular proton transfer supramolecular interactions Biology (General) QH301-705.5 Chemistry QD1-999
spellingShingle	inclusion complex bovine serum albumin tryptophan excited-state intramolecular proton transfer supramolecular interactions Biology (General) QH301-705.5 Chemistry QD1-999 Karolina Baranowska Michał Mońka Piotr Bojarski Marek Józefowicz Insight into Molecular Interactions of Two Methyl Benzoate Derivatives with Bovine Serum Albumin
description	The nature and mechanisms of interaction between two selected methyl benzoate derivatives (methyl <i>o</i>-methoxy <i>p</i>-methylaminobenzoate–<b>I</b> and methyl <i>o</i>-hydroxy <i>p</i>-methylaminobenzoate–<b>II</b>) and model transport protein bovine serum albumin (BSA) was studied using steady-state and time-resolved spectroscopic techniques. In order to understand the role of Trp residue of BSA in the <b>I</b>-BSA and <b>II</b>-BSA interaction, the effect of free Trp amino acid on the both emission modes (LE–locally excited (<b>I</b> and <b>II</b>) and ESIPT–excited state intramolecular proton transfer (<b>II</b>)) was investigated as well. Experimental results show that the investigated interactions (with both BSA and Trp) are mostly conditioned by the ground and excited state complex formation processes. Both molecules form stable complexes with BSA and Trp (with 1:1 stoichiometry) in the ground and excited states. The binding constants were in the order of 10<sup>4</sup> M<sup>−1</sup>. The absorption- and fluorescence-titration experiments along with the time-resolved fluorescence measurements show that the binding of the <b>I</b> and <b>II</b> causes fluorescence quenching of BSA through the static mechanism, revealing a 1:1 interaction. The magnitude and the sign of the thermodynamic parameters, Δ<i>H</i>, Δ<i>S</i>, and Δ<i>G</i>, determined from van’t Hoff relationship, confirm the predominance of the hydrogen-bonding interactions for the binding phenomenon. To improve and complete knowledge of methyl benzoate derivative-protein interactions in relation to supramolecular solvation dynamics, the time-dependent fluorescence Stokes’ shifts, represented by the normalized spectral response function <i>c(t)</i>, was studied. Our studies reveal that the solvation dynamics that occurs in subpicosecond time scale in neat solvents of different polarities is slowed down significantly when the organic molecule is transferred to BSA cavity.
format	article
author	Karolina Baranowska Michał Mońka Piotr Bojarski Marek Józefowicz
author_facet	Karolina Baranowska Michał Mońka Piotr Bojarski Marek Józefowicz
author_sort	Karolina Baranowska
title	Insight into Molecular Interactions of Two Methyl Benzoate Derivatives with Bovine Serum Albumin
title_short	Insight into Molecular Interactions of Two Methyl Benzoate Derivatives with Bovine Serum Albumin
title_full	Insight into Molecular Interactions of Two Methyl Benzoate Derivatives with Bovine Serum Albumin
title_fullStr	Insight into Molecular Interactions of Two Methyl Benzoate Derivatives with Bovine Serum Albumin
title_full_unstemmed	Insight into Molecular Interactions of Two Methyl Benzoate Derivatives with Bovine Serum Albumin
title_sort	insight into molecular interactions of two methyl benzoate derivatives with bovine serum albumin
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/a53cd76ee3a8468f81b3ccb33a4e91a9
work_keys_str_mv	AT karolinabaranowska insightintomolecularinteractionsoftwomethylbenzoatederivativeswithbovineserumalbumin AT michałmonka insightintomolecularinteractionsoftwomethylbenzoatederivativeswithbovineserumalbumin AT piotrbojarski insightintomolecularinteractionsoftwomethylbenzoatederivativeswithbovineserumalbumin AT marekjozefowicz insightintomolecularinteractionsoftwomethylbenzoatederivativeswithbovineserumalbumin
_version_	1718432194097053696

Insight into Molecular Interactions of Two Methyl Benzoate Derivatives with Bovine Serum Albumin

Ejemplares similares