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Mechanistic interaction study of 5,6-Dichloro-2-[2-(pyridin-2-yl)ethyl]isoindoline-1,3-dione with bovine serum albumin by spectroscopic and molecular docking approaches

A synthesized and promising biologically hypoglycemic compound 5,6-Dichloro-2-[2-(pyridin-2-yl)ethyl]isoindoline-1,3-dione (5e) was studied for its binding to a model protein (bovine serum albumin; BSA) by spectroscopic and molecular simulation approaches. Fluorescence studies revealed that 5e quenc...

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Autores principales: Alanazi, Mohammed M., Almehizia, Abdulrahman A., Bakheit, Ahmed H., Alsaif, Nawaf A., Alkahtani, Hamad M., Wani, Tanveer A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6438701/
https://www.ncbi.nlm.nih.gov/pubmed/30976176
http://dx.doi.org/10.1016/j.jsps.2018.12.001
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author Alanazi, Mohammed M.
Almehizia, Abdulrahman A.
Bakheit, Ahmed H.
Alsaif, Nawaf A.
Alkahtani, Hamad M.
Wani, Tanveer A.
author_facet Alanazi, Mohammed M.
Almehizia, Abdulrahman A.
Bakheit, Ahmed H.
Alsaif, Nawaf A.
Alkahtani, Hamad M.
Wani, Tanveer A.
author_sort Alanazi, Mohammed M.
collection PubMed
description A synthesized and promising biologically hypoglycemic compound 5,6-Dichloro-2-[2-(pyridin-2-yl)ethyl]isoindoline-1,3-dione (5e) was studied for its binding to a model protein (bovine serum albumin; BSA) by spectroscopic and molecular simulation approaches. Fluorescence studies revealed that 5e quenched BSA’s intrinsic fluorescence by static quenching. The experiments were performed at three different temperatures and the quenching constants and binding constants were evaluated. Stern-Volmer constant (K(sv)) values decreased from 1.36 × 10(4) to 1.20 × 10(4) as the temperature increased suggesting static quenching involvement in the interaction. Decreased binding constants from 1.70 × 10(4) to 4.57 × 10(3) at higher temperatures indicated instability of the complex at rising temperatures. Site I (subdomain IIA) of BSA was found to interact with 5e. The thermodynamic results showed the binding interaction was spontaneous and enthalpy driven. The secondary structure alterations in BSA due to interaction with 5e were studied by UV–visible, synchronous fluorescence, and three-dimensional fluorescence spectra. The results indicate the 5e binds effectively to the BSA and thus, this study can be useful in further exploring the pharmacokinetics and pharmacodynamics of 5e.
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spelling pubmed-64387012019-04-11 Mechanistic interaction study of 5,6-Dichloro-2-[2-(pyridin-2-yl)ethyl]isoindoline-1,3-dione with bovine serum albumin by spectroscopic and molecular docking approaches Alanazi, Mohammed M. Almehizia, Abdulrahman A. Bakheit, Ahmed H. Alsaif, Nawaf A. Alkahtani, Hamad M. Wani, Tanveer A. Saudi Pharm J Article A synthesized and promising biologically hypoglycemic compound 5,6-Dichloro-2-[2-(pyridin-2-yl)ethyl]isoindoline-1,3-dione (5e) was studied for its binding to a model protein (bovine serum albumin; BSA) by spectroscopic and molecular simulation approaches. Fluorescence studies revealed that 5e quenched BSA’s intrinsic fluorescence by static quenching. The experiments were performed at three different temperatures and the quenching constants and binding constants were evaluated. Stern-Volmer constant (K(sv)) values decreased from 1.36 × 10(4) to 1.20 × 10(4) as the temperature increased suggesting static quenching involvement in the interaction. Decreased binding constants from 1.70 × 10(4) to 4.57 × 10(3) at higher temperatures indicated instability of the complex at rising temperatures. Site I (subdomain IIA) of BSA was found to interact with 5e. The thermodynamic results showed the binding interaction was spontaneous and enthalpy driven. The secondary structure alterations in BSA due to interaction with 5e were studied by UV–visible, synchronous fluorescence, and three-dimensional fluorescence spectra. The results indicate the 5e binds effectively to the BSA and thus, this study can be useful in further exploring the pharmacokinetics and pharmacodynamics of 5e. Elsevier 2019-03 2018-12-06 /pmc/articles/PMC6438701/ /pubmed/30976176 http://dx.doi.org/10.1016/j.jsps.2018.12.001 Text en © 2018 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Article
Alanazi, Mohammed M.
Almehizia, Abdulrahman A.
Bakheit, Ahmed H.
Alsaif, Nawaf A.
Alkahtani, Hamad M.
Wani, Tanveer A.
Mechanistic interaction study of 5,6-Dichloro-2-[2-(pyridin-2-yl)ethyl]isoindoline-1,3-dione with bovine serum albumin by spectroscopic and molecular docking approaches
title Mechanistic interaction study of 5,6-Dichloro-2-[2-(pyridin-2-yl)ethyl]isoindoline-1,3-dione with bovine serum albumin by spectroscopic and molecular docking approaches
title_full Mechanistic interaction study of 5,6-Dichloro-2-[2-(pyridin-2-yl)ethyl]isoindoline-1,3-dione with bovine serum albumin by spectroscopic and molecular docking approaches
title_fullStr Mechanistic interaction study of 5,6-Dichloro-2-[2-(pyridin-2-yl)ethyl]isoindoline-1,3-dione with bovine serum albumin by spectroscopic and molecular docking approaches
title_full_unstemmed Mechanistic interaction study of 5,6-Dichloro-2-[2-(pyridin-2-yl)ethyl]isoindoline-1,3-dione with bovine serum albumin by spectroscopic and molecular docking approaches
title_short Mechanistic interaction study of 5,6-Dichloro-2-[2-(pyridin-2-yl)ethyl]isoindoline-1,3-dione with bovine serum albumin by spectroscopic and molecular docking approaches
title_sort mechanistic interaction study of 5,6-dichloro-2-[2-(pyridin-2-yl)ethyl]isoindoline-1,3-dione with bovine serum albumin by spectroscopic and molecular docking approaches
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6438701/
https://www.ncbi.nlm.nih.gov/pubmed/30976176
http://dx.doi.org/10.1016/j.jsps.2018.12.001
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