Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin

The binding interactions of bovine serum albumin (BSA) with tetraphenylborate ions ([B(Ph)<sub>4</sub>]<sup>−</sup>) have been investigated by a set of experimental methods (isothermal titration calorimetry, steady-state fluorescence spectroscopy, differential scanning calori...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Ola Grabowska, Małgorzata M. Kogut, Krzysztof Żamojć, Sergey A. Samsonov, Joanna Makowska, Aleksandra Tesmar, Katarzyna Chmur, Dariusz Wyrzykowski, Lech Chmurzyński
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	bovine serum albumin sodium tetraphenylborate sodium dodecyl sulfate binding site thermodynamic parameters Organic chemistry QD241-441
Acceso en línea:	https://doaj.org/article/f8050874dd1e496c8b2ce31d97167efa
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:f8050874dd1e496c8b2ce31d97167efa
record_format	dspace
spelling	oai:doaj.org-article:f8050874dd1e496c8b2ce31d97167efa2021-11-11T18:32:51ZEffect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin10.3390/molecules262165651420-3049https://doaj.org/article/f8050874dd1e496c8b2ce31d97167efa2021-10-01T00:00:00Zhttps://www.mdpi.com/1420-3049/26/21/6565https://doaj.org/toc/1420-3049The binding interactions of bovine serum albumin (BSA) with tetraphenylborate ions ([B(Ph)<sub>4</sub>]<sup>−</sup>) have been investigated by a set of experimental methods (isothermal titration calorimetry, steady-state fluorescence spectroscopy, differential scanning calorimetry and circular dichroism spectroscopy) and molecular dynamics-based computational approaches. Two sets of structurally distinctive binding sites in BSA were found under the experimental conditions (10 mM cacodylate buffer, pH 7, 298.15 K). The obtained results, supported by the competitive interactions experiments of SDS with [B(Ph)<sub>4</sub>]<sup>−</sup> for BSA, enabled us to find the potential binding sites in BSA. The first site is located in the subdomain I A of the protein and binds two [B(Ph)<sub>4</sub>]<sup>−</sup> ions (log<i>K</i><sub>(ITC)1</sub> = 7.09 ± 0.10; Δ<i>G</i><sub>(ITC)1</sub> = −9.67 ± 0.14 kcal mol<sup>−1</sup>; Δ<i>H</i><sub>(ITC)1</sub> = −3.14 ± 0.12 kcal mol<sup>−1</sup>; TΔ<i>S</i><sub>(ITC)1</sub> = −6.53 kcal mol<sup>−1</sup>), whereas the second site is localized in the subdomain III A and binds five ions (log<i>K</i><sub>(ITC)2</sub> = 5.39 ± 0.06; Δ<i>G</i><sub>(ITC)2</sub> = −7.35 ± 0.09 kcal mol<sup>−1</sup>; Δ<i>H</i><sub>(ITC)2</sub> = 4.00 ± 0.14 kcal mol<sup>−1</sup>; TΔ<i>S</i><sub>(ITC)2</sub> = 11.3 kcal mol<sup>−1</sup>). The formation of the {[B(Ph)<sub>4</sub>]<sup>−</sup>}–BSA complex results in an increase in the thermal stability of the alfa-helical content, correlating with the saturation of the particular BSA binding sites, thus hindering its thermal unfolding.Ola GrabowskaMałgorzata M. KogutKrzysztof ŻamojćSergey A. SamsonovJoanna MakowskaAleksandra TesmarKatarzyna ChmurDariusz WyrzykowskiLech ChmurzyńskiMDPI AGarticlebovine serum albuminsodium tetraphenylboratesodium dodecyl sulfatebinding sitethermodynamic parametersOrganic chemistryQD241-441ENMolecules, Vol 26, Iss 6565, p 6565 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	bovine serum albumin sodium tetraphenylborate sodium dodecyl sulfate binding site thermodynamic parameters Organic chemistry QD241-441
spellingShingle	bovine serum albumin sodium tetraphenylborate sodium dodecyl sulfate binding site thermodynamic parameters Organic chemistry QD241-441 Ola Grabowska Małgorzata M. Kogut Krzysztof Żamojć Sergey A. Samsonov Joanna Makowska Aleksandra Tesmar Katarzyna Chmur Dariusz Wyrzykowski Lech Chmurzyński Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin
description	The binding interactions of bovine serum albumin (BSA) with tetraphenylborate ions ([B(Ph)<sub>4</sub>]<sup>−</sup>) have been investigated by a set of experimental methods (isothermal titration calorimetry, steady-state fluorescence spectroscopy, differential scanning calorimetry and circular dichroism spectroscopy) and molecular dynamics-based computational approaches. Two sets of structurally distinctive binding sites in BSA were found under the experimental conditions (10 mM cacodylate buffer, pH 7, 298.15 K). The obtained results, supported by the competitive interactions experiments of SDS with [B(Ph)<sub>4</sub>]<sup>−</sup> for BSA, enabled us to find the potential binding sites in BSA. The first site is located in the subdomain I A of the protein and binds two [B(Ph)<sub>4</sub>]<sup>−</sup> ions (log<i>K</i><sub>(ITC)1</sub> = 7.09 ± 0.10; Δ<i>G</i><sub>(ITC)1</sub> = −9.67 ± 0.14 kcal mol<sup>−1</sup>; Δ<i>H</i><sub>(ITC)1</sub> = −3.14 ± 0.12 kcal mol<sup>−1</sup>; TΔ<i>S</i><sub>(ITC)1</sub> = −6.53 kcal mol<sup>−1</sup>), whereas the second site is localized in the subdomain III A and binds five ions (log<i>K</i><sub>(ITC)2</sub> = 5.39 ± 0.06; Δ<i>G</i><sub>(ITC)2</sub> = −7.35 ± 0.09 kcal mol<sup>−1</sup>; Δ<i>H</i><sub>(ITC)2</sub> = 4.00 ± 0.14 kcal mol<sup>−1</sup>; TΔ<i>S</i><sub>(ITC)2</sub> = 11.3 kcal mol<sup>−1</sup>). The formation of the {[B(Ph)<sub>4</sub>]<sup>−</sup>}–BSA complex results in an increase in the thermal stability of the alfa-helical content, correlating with the saturation of the particular BSA binding sites, thus hindering its thermal unfolding.
format	article
author	Ola Grabowska Małgorzata M. Kogut Krzysztof Żamojć Sergey A. Samsonov Joanna Makowska Aleksandra Tesmar Katarzyna Chmur Dariusz Wyrzykowski Lech Chmurzyński
author_facet	Ola Grabowska Małgorzata M. Kogut Krzysztof Żamojć Sergey A. Samsonov Joanna Makowska Aleksandra Tesmar Katarzyna Chmur Dariusz Wyrzykowski Lech Chmurzyński
author_sort	Ola Grabowska
title	Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin
title_short	Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin
title_full	Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin
title_fullStr	Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin
title_full_unstemmed	Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin
title_sort	effect of tetraphenylborate on physicochemical properties of bovine serum albumin
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/f8050874dd1e496c8b2ce31d97167efa
work_keys_str_mv	AT olagrabowska effectoftetraphenylborateonphysicochemicalpropertiesofbovineserumalbumin AT małgorzatamkogut effectoftetraphenylborateonphysicochemicalpropertiesofbovineserumalbumin AT krzysztofzamojc effectoftetraphenylborateonphysicochemicalpropertiesofbovineserumalbumin AT sergeyasamsonov effectoftetraphenylborateonphysicochemicalpropertiesofbovineserumalbumin AT joannamakowska effectoftetraphenylborateonphysicochemicalpropertiesofbovineserumalbumin AT aleksandratesmar effectoftetraphenylborateonphysicochemicalpropertiesofbovineserumalbumin AT katarzynachmur effectoftetraphenylborateonphysicochemicalpropertiesofbovineserumalbumin AT dariuszwyrzykowski effectoftetraphenylborateonphysicochemicalpropertiesofbovineserumalbumin AT lechchmurzynski effectoftetraphenylborateonphysicochemicalpropertiesofbovineserumalbumin
_version_	1718431799463378944

Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin

Ejemplares similares