Multispectroscopic and molecular modeling strategy to explore the interaction of cholest-5-en-7-one with human serum albumin: DFT and Hirshfeld surface analysis

The present study accounts for cholest-5-en-7-one (steroid) synthesis using selenium dioxide and silica as well as its identification using high-resolution mass spectrometry (HRMS), FT-IR, NMR, and elemental analysis. Density functional theory (DFT) calculations were used to optimize the steroid...

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Autor principal:	Mahboob Alam
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	MD simulations Steroid Spectroscopy DFT Molecular docking Science (General) Q1-390
Acceso en línea:	https://doaj.org/article/3e05616b286e419bb3387d0c227c27ba
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spelling	oai:doaj.org-article:3e05616b286e419bb3387d0c227c27ba2021-11-18T04:44:30ZMultispectroscopic and molecular modeling strategy to explore the interaction of cholest-5-en-7-one with human serum albumin: DFT and Hirshfeld surface analysis1018-364710.1016/j.jksus.2021.101661https://doaj.org/article/3e05616b286e419bb3387d0c227c27ba2021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S1018364721003232https://doaj.org/toc/1018-3647The present study accounts for cholest-5-en-7-one (steroid) synthesis using selenium dioxide and silica as well as its identification using high-resolution mass spectrometry (HRMS), FT-IR, NMR, and elemental analysis. Density functional theory (DFT) calculations were used to optimize the steroid's geometry, which was then compared to single-crystal X-ray diffraction data, indicating that the computational and experimental results were in good agreement. UV–vis absorption titration, fluorescence spectral methods, circular dichroism (CD), and dynamic light scattering (DLS) were used to investigate the well-identified steroid's in vitro molecular interaction with human serum albumin (HSA). The results and binding parameter indicate that the steroid has significant binding affinity for HSA. Molecular docking was performed and found that the steroid can interact with the hydrophobic cavity of HSA through hydrogen and hydrophobic contacts. Molecular dynamics simulation was used to confirm the stability of the HSA-steroid complex. Combined quantum mechanics-molecular mechanics (QM-MM) methods were applied to know binding energy of system and individual components for atomic level interactions indicating a significant interaction between the steroid and the biomacromolecules. The findings presented here contribute to a better understanding of steroid pharmacodynamics.Mahboob AlamElsevierarticleMD simulationsSteroidSpectroscopyDFTMolecular dockingScience (General)Q1-390ENJournal of King Saud University: Science, Vol 33, Iss 8, Pp 101661- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	MD simulations Steroid Spectroscopy DFT Molecular docking Science (General) Q1-390
spellingShingle	MD simulations Steroid Spectroscopy DFT Molecular docking Science (General) Q1-390 Mahboob Alam Multispectroscopic and molecular modeling strategy to explore the interaction of cholest-5-en-7-one with human serum albumin: DFT and Hirshfeld surface analysis
description	The present study accounts for cholest-5-en-7-one (steroid) synthesis using selenium dioxide and silica as well as its identification using high-resolution mass spectrometry (HRMS), FT-IR, NMR, and elemental analysis. Density functional theory (DFT) calculations were used to optimize the steroid's geometry, which was then compared to single-crystal X-ray diffraction data, indicating that the computational and experimental results were in good agreement. UV–vis absorption titration, fluorescence spectral methods, circular dichroism (CD), and dynamic light scattering (DLS) were used to investigate the well-identified steroid's in vitro molecular interaction with human serum albumin (HSA). The results and binding parameter indicate that the steroid has significant binding affinity for HSA. Molecular docking was performed and found that the steroid can interact with the hydrophobic cavity of HSA through hydrogen and hydrophobic contacts. Molecular dynamics simulation was used to confirm the stability of the HSA-steroid complex. Combined quantum mechanics-molecular mechanics (QM-MM) methods were applied to know binding energy of system and individual components for atomic level interactions indicating a significant interaction between the steroid and the biomacromolecules. The findings presented here contribute to a better understanding of steroid pharmacodynamics.
format	article
author	Mahboob Alam
author_facet	Mahboob Alam
author_sort	Mahboob Alam
title	Multispectroscopic and molecular modeling strategy to explore the interaction of cholest-5-en-7-one with human serum albumin: DFT and Hirshfeld surface analysis
title_short	Multispectroscopic and molecular modeling strategy to explore the interaction of cholest-5-en-7-one with human serum albumin: DFT and Hirshfeld surface analysis
title_full	Multispectroscopic and molecular modeling strategy to explore the interaction of cholest-5-en-7-one with human serum albumin: DFT and Hirshfeld surface analysis
title_fullStr	Multispectroscopic and molecular modeling strategy to explore the interaction of cholest-5-en-7-one with human serum albumin: DFT and Hirshfeld surface analysis
title_full_unstemmed	Multispectroscopic and molecular modeling strategy to explore the interaction of cholest-5-en-7-one with human serum albumin: DFT and Hirshfeld surface analysis
title_sort	multispectroscopic and molecular modeling strategy to explore the interaction of cholest-5-en-7-one with human serum albumin: dft and hirshfeld surface analysis
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/3e05616b286e419bb3387d0c227c27ba
work_keys_str_mv	AT mahboobalam multispectroscopicandmolecularmodelingstrategytoexploretheinteractionofcholest5en7onewithhumanserumalbumindftandhirshfeldsurfaceanalysis
_version_	1718425093111021568

Multispectroscopic and molecular modeling strategy to explore the interaction of cholest-5-en-7-one with human serum albumin: DFT and Hirshfeld surface analysis

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