Interaction Study between ESIPT Fluorescent Lipophile-Based Benzazoles and BSA

In this study, the interactions of ESIPT fluorescent lipophile-based benzazoles with bovine serum albumin (BSA) were studied and their binding affinity was evaluated. In phosphate-buffered saline (PBS) solution these compounds produce absorption maxima in the UV region and a main fluorescence emissi...

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Autores principales:	Thais Kroetz, Pablo Andrei Nogara, Fabiano da Silveira Santos, Lilian Camargo da Luz, Viktor Saraiva Câmara, João Batista Teixeira da Rocha, Alexandre Gonçalves Dal-Bó, Fabiano Severo Rodembusch
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	benzazoles proton transfer bovine serum albumin fluorescence quenching molecular docking Organic chemistry QD241-441
Acceso en línea:	https://doaj.org/article/4afa70aac0f444d6b76cadc99187c828
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id	oai:doaj.org-article:4afa70aac0f444d6b76cadc99187c828
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spelling	oai:doaj.org-article:4afa70aac0f444d6b76cadc99187c8282021-11-11T18:39:58ZInteraction Study between ESIPT Fluorescent Lipophile-Based Benzazoles and BSA10.3390/molecules262167281420-3049https://doaj.org/article/4afa70aac0f444d6b76cadc99187c8282021-11-01T00:00:00Zhttps://www.mdpi.com/1420-3049/26/21/6728https://doaj.org/toc/1420-3049In this study, the interactions of ESIPT fluorescent lipophile-based benzazoles with bovine serum albumin (BSA) were studied and their binding affinity was evaluated. In phosphate-buffered saline (PBS) solution these compounds produce absorption maxima in the UV region and a main fluorescence emission with a large Stokes shift in the blue–green regions due to a proton transfer process in the excited state. The interactions of the benzazoles with BSA were studied using UV-Vis absorption and steady-state fluorescence spectroscopy. The observed spectral quenching of BSA indicates that these compounds could bind to BSA through a strong binding affinity afforded by a static quenching mechanism (K<sub>q</sub>~10<sup>12</sup> L·mol<sup>−1</sup>·s<sup>−1</sup>). The docking simulations indicate that compounds <b>13</b> and <b>16</b> bind closely to Trp134 in domain I, adopting similar binding poses and interactions. On the other hand, compounds <b>12</b>, <b>14</b>, <b>15</b>, and <b>17</b> were bound between domains I and III and did not directly interact with Trp134.Thais KroetzPablo Andrei NogaraFabiano da Silveira SantosLilian Camargo da LuzViktor Saraiva CâmaraJoão Batista Teixeira da RochaAlexandre Gonçalves Dal-BóFabiano Severo RodembuschMDPI AGarticlebenzazolesproton transferbovine serum albuminfluorescence quenchingmolecular dockingOrganic chemistryQD241-441ENMolecules, Vol 26, Iss 6728, p 6728 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	benzazoles proton transfer bovine serum albumin fluorescence quenching molecular docking Organic chemistry QD241-441
spellingShingle	benzazoles proton transfer bovine serum albumin fluorescence quenching molecular docking Organic chemistry QD241-441 Thais Kroetz Pablo Andrei Nogara Fabiano da Silveira Santos Lilian Camargo da Luz Viktor Saraiva Câmara João Batista Teixeira da Rocha Alexandre Gonçalves Dal-Bó Fabiano Severo Rodembusch Interaction Study between ESIPT Fluorescent Lipophile-Based Benzazoles and BSA
description	In this study, the interactions of ESIPT fluorescent lipophile-based benzazoles with bovine serum albumin (BSA) were studied and their binding affinity was evaluated. In phosphate-buffered saline (PBS) solution these compounds produce absorption maxima in the UV region and a main fluorescence emission with a large Stokes shift in the blue–green regions due to a proton transfer process in the excited state. The interactions of the benzazoles with BSA were studied using UV-Vis absorption and steady-state fluorescence spectroscopy. The observed spectral quenching of BSA indicates that these compounds could bind to BSA through a strong binding affinity afforded by a static quenching mechanism (K<sub>q</sub>~10<sup>12</sup> L·mol<sup>−1</sup>·s<sup>−1</sup>). The docking simulations indicate that compounds <b>13</b> and <b>16</b> bind closely to Trp134 in domain I, adopting similar binding poses and interactions. On the other hand, compounds <b>12</b>, <b>14</b>, <b>15</b>, and <b>17</b> were bound between domains I and III and did not directly interact with Trp134.
format	article
author	Thais Kroetz Pablo Andrei Nogara Fabiano da Silveira Santos Lilian Camargo da Luz Viktor Saraiva Câmara João Batista Teixeira da Rocha Alexandre Gonçalves Dal-Bó Fabiano Severo Rodembusch
author_facet	Thais Kroetz Pablo Andrei Nogara Fabiano da Silveira Santos Lilian Camargo da Luz Viktor Saraiva Câmara João Batista Teixeira da Rocha Alexandre Gonçalves Dal-Bó Fabiano Severo Rodembusch
author_sort	Thais Kroetz
title	Interaction Study between ESIPT Fluorescent Lipophile-Based Benzazoles and BSA
title_short	Interaction Study between ESIPT Fluorescent Lipophile-Based Benzazoles and BSA
title_full	Interaction Study between ESIPT Fluorescent Lipophile-Based Benzazoles and BSA
title_fullStr	Interaction Study between ESIPT Fluorescent Lipophile-Based Benzazoles and BSA
title_full_unstemmed	Interaction Study between ESIPT Fluorescent Lipophile-Based Benzazoles and BSA
title_sort	interaction study between esipt fluorescent lipophile-based benzazoles and bsa
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/4afa70aac0f444d6b76cadc99187c828
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Interaction Study between ESIPT Fluorescent Lipophile-Based Benzazoles and BSA

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