Preferential binding of fullerene and fullerenol with the N-terminal and middle regions of amyloid beta peptide: an in silico investigation

Vishal Pandya,1 Lokesh Baweja,1,2 Alok Dhawan1,2 1Division of Biological & Life Sciences, School of Arts & Sciences, (Formerly, Institute of Life Sciences), Ahmedabad University, Ahmedabad, Gujarat, 2Nanotherapeutics & Nanomaterial Toxicology Group, CSIR-Indian Institute of...

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Autores principales:	Pandya V, Baweja L, Dhawan A
Formato:	article
Lenguaje:	EN
Publicado:	Dove Medical Press 2018
Materias:	Nanoparticles Amyloid beta docking Medicine (General) R5-920
Acceso en línea:	https://doaj.org/article/88dce8a9e2fd4c0385976dec1aa50623
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spelling	oai:doaj.org-article:88dce8a9e2fd4c0385976dec1aa506232021-12-02T02:52:35ZPreferential binding of fullerene and fullerenol with the N-terminal and middle regions of amyloid beta peptide: an in silico investigation1178-2013https://doaj.org/article/88dce8a9e2fd4c0385976dec1aa506232018-03-01T00:00:00Zhttps://www.dovepress.com/preferential-binding-of-fullerene-and-fullerenol-with-the-n-terminal-a-peer-reviewed-article-IJNhttps://doaj.org/toc/1178-2013Vishal Pandya,1 Lokesh Baweja,1,2 Alok Dhawan1,2 1Division of Biological & Life Sciences, School of Arts & Sciences, (Formerly, Institute of Life Sciences), Ahmedabad University, Ahmedabad, Gujarat, 2Nanotherapeutics & Nanomaterial Toxicology Group, CSIR-Indian Institute of Toxicology Research, Mahatma Gandhi Marg, Lucknow, Uttar Pradesh, India Abstract: Amyloid beta (Aβ) deposits are implicated in the pathogenesis of debilitating neurodegenerative disorders such as Alzheimer’s disease. In the present study, the interactions of carbon-based nanoparticles (NPs) such as fullerene and fullerenol having different surface chemistry with Aβ were investigated using molecular dynamics simulations and docking studies. A detailed analysis of docking results showed that in 68% of the Aβ conformations, fullerene and fullerenol showed interactions with the N-terminal region of the peptide. However, the high-affinity binding site (E=−48.31 kJ/mol) of fullerene resides in the hydrophobic middle region of the peptide, whereas fullerenol interacts favorably with the charged N-terminal region with a binding energy of −50.42 kJ/mol. The above differences in binding could be attributed to the surface chemistry of fullerene and fullerenol. Moreover, the N-terminal and middle regions of Aβ play an important role in Aβ aggregation. Therefore, the binding of fullerene and fullerenol could inhibit amyloid aggregation. This information will be helpful in designing NPs for targeting amyloid-related disorders. Keywords: fullerene, fullerenolPandya VBaweja LDhawan ADove Medical PressarticleNanoparticlesAmyloid betadockingMedicine (General)R5-920ENInternational Journal of Nanomedicine, Vol Volume 13, Pp 71-73 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Nanoparticles Amyloid beta docking Medicine (General) R5-920
spellingShingle	Nanoparticles Amyloid beta docking Medicine (General) R5-920 Pandya V Baweja L Dhawan A Preferential binding of fullerene and fullerenol with the N-terminal and middle regions of amyloid beta peptide: an in silico investigation
description	Vishal Pandya,1 Lokesh Baweja,1,2 Alok Dhawan1,2 1Division of Biological & Life Sciences, School of Arts & Sciences, (Formerly, Institute of Life Sciences), Ahmedabad University, Ahmedabad, Gujarat, 2Nanotherapeutics & Nanomaterial Toxicology Group, CSIR-Indian Institute of Toxicology Research, Mahatma Gandhi Marg, Lucknow, Uttar Pradesh, India Abstract: Amyloid beta (Aβ) deposits are implicated in the pathogenesis of debilitating neurodegenerative disorders such as Alzheimer’s disease. In the present study, the interactions of carbon-based nanoparticles (NPs) such as fullerene and fullerenol having different surface chemistry with Aβ were investigated using molecular dynamics simulations and docking studies. A detailed analysis of docking results showed that in 68% of the Aβ conformations, fullerene and fullerenol showed interactions with the N-terminal region of the peptide. However, the high-affinity binding site (E=−48.31 kJ/mol) of fullerene resides in the hydrophobic middle region of the peptide, whereas fullerenol interacts favorably with the charged N-terminal region with a binding energy of −50.42 kJ/mol. The above differences in binding could be attributed to the surface chemistry of fullerene and fullerenol. Moreover, the N-terminal and middle regions of Aβ play an important role in Aβ aggregation. Therefore, the binding of fullerene and fullerenol could inhibit amyloid aggregation. This information will be helpful in designing NPs for targeting amyloid-related disorders. Keywords: fullerene, fullerenol
format	article
author	Pandya V Baweja L Dhawan A
author_facet	Pandya V Baweja L Dhawan A
author_sort	Pandya V
title	Preferential binding of fullerene and fullerenol with the N-terminal and middle regions of amyloid beta peptide: an in silico investigation
title_short	Preferential binding of fullerene and fullerenol with the N-terminal and middle regions of amyloid beta peptide: an in silico investigation
title_full	Preferential binding of fullerene and fullerenol with the N-terminal and middle regions of amyloid beta peptide: an in silico investigation
title_fullStr	Preferential binding of fullerene and fullerenol with the N-terminal and middle regions of amyloid beta peptide: an in silico investigation
title_full_unstemmed	Preferential binding of fullerene and fullerenol with the N-terminal and middle regions of amyloid beta peptide: an in silico investigation
title_sort	preferential binding of fullerene and fullerenol with the n-terminal and middle regions of amyloid beta peptide: an in silico investigation
publisher	Dove Medical Press
publishDate	2018
url	https://doaj.org/article/88dce8a9e2fd4c0385976dec1aa50623
work_keys_str_mv	AT pandyav preferentialbindingoffullereneandfullerenolwiththenterminalandmiddleregionsofamyloidbetapeptideaninsilicoinvestigation AT bawejal preferentialbindingoffullereneandfullerenolwiththenterminalandmiddleregionsofamyloidbetapeptideaninsilicoinvestigation AT dhawana preferentialbindingoffullereneandfullerenolwiththenterminalandmiddleregionsofamyloidbetapeptideaninsilicoinvestigation
_version_	1718402111628115968

Preferential binding of fullerene and fullerenol with the N-terminal and middle regions of amyloid beta peptide: an in silico investigation

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