The computational analyses, molecular dynamics of fatty-acid transport mechanism to the CD36 receptor

Abstract The transmembrane glycoprotein CD36, which is responsible of the metabolic disorders, and the elevated intake of fat induces lipid buildup, is a multifunctional scavenger receptor signaling those functions in high-affinity tissue uptake of long-chain fatty acids. In this study, we used seri...

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Autores principales:	Jihane Akachar, Catherine Etchebest, Rachid El Jaoudi, Azeddine Ibrahimi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/2b5dd3eac14049f89887d5c042baf505
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spelling	oai:doaj.org-article:2b5dd3eac14049f89887d5c042baf5052021-12-05T12:11:35ZThe computational analyses, molecular dynamics of fatty-acid transport mechanism to the CD36 receptor10.1038/s41598-021-01373-52045-2322https://doaj.org/article/2b5dd3eac14049f89887d5c042baf5052021-12-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-01373-5https://doaj.org/toc/2045-2322Abstract The transmembrane glycoprotein CD36, which is responsible of the metabolic disorders, and the elevated intake of fat induces lipid buildup, is a multifunctional scavenger receptor signaling those functions in high-affinity tissue uptake of long-chain fatty acids. In this study, we used series of molecular dynamics simulations of the wild type and mutants types K164A CD36 protein interacting with one palmitic acid (PLM) besides simulations of the wild type interacting with the three PLM to find out the mechanism of the functioning of the complex CD36/Fatty acids and the unraveling of the role of the mutation. Additionally we determined whether Lys164, mostly exposed to protein surface, played important roles in fatty acid uptake. These simulations revealed, the conformational changes induced by Lys164 residue and the altered interactions induced by the mutagenesis of surface lysine that was badly influencing the folding, utility, solubility, and stability form of the variant. Furthermore, Lys164 residue provided the structural basis of forming an opening at the region of principal portal for the dissociation of palmitic acid. The results of our simulations revealed hole two fatty acids found in CD36 cavity structure and it was the most preferred to CD36 structure stabilization.Jihane AkacharCatherine EtchebestRachid El JaoudiAzeddine IbrahimiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jihane Akachar Catherine Etchebest Rachid El Jaoudi Azeddine Ibrahimi The computational analyses, molecular dynamics of fatty-acid transport mechanism to the CD36 receptor
description	Abstract The transmembrane glycoprotein CD36, which is responsible of the metabolic disorders, and the elevated intake of fat induces lipid buildup, is a multifunctional scavenger receptor signaling those functions in high-affinity tissue uptake of long-chain fatty acids. In this study, we used series of molecular dynamics simulations of the wild type and mutants types K164A CD36 protein interacting with one palmitic acid (PLM) besides simulations of the wild type interacting with the three PLM to find out the mechanism of the functioning of the complex CD36/Fatty acids and the unraveling of the role of the mutation. Additionally we determined whether Lys164, mostly exposed to protein surface, played important roles in fatty acid uptake. These simulations revealed, the conformational changes induced by Lys164 residue and the altered interactions induced by the mutagenesis of surface lysine that was badly influencing the folding, utility, solubility, and stability form of the variant. Furthermore, Lys164 residue provided the structural basis of forming an opening at the region of principal portal for the dissociation of palmitic acid. The results of our simulations revealed hole two fatty acids found in CD36 cavity structure and it was the most preferred to CD36 structure stabilization.
format	article
author	Jihane Akachar Catherine Etchebest Rachid El Jaoudi Azeddine Ibrahimi
author_facet	Jihane Akachar Catherine Etchebest Rachid El Jaoudi Azeddine Ibrahimi
author_sort	Jihane Akachar
title	The computational analyses, molecular dynamics of fatty-acid transport mechanism to the CD36 receptor
title_short	The computational analyses, molecular dynamics of fatty-acid transport mechanism to the CD36 receptor
title_full	The computational analyses, molecular dynamics of fatty-acid transport mechanism to the CD36 receptor
title_fullStr	The computational analyses, molecular dynamics of fatty-acid transport mechanism to the CD36 receptor
title_full_unstemmed	The computational analyses, molecular dynamics of fatty-acid transport mechanism to the CD36 receptor
title_sort	computational analyses, molecular dynamics of fatty-acid transport mechanism to the cd36 receptor
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/2b5dd3eac14049f89887d5c042baf505
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The computational analyses, molecular dynamics of fatty-acid transport mechanism to the CD36 receptor

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