Effect of gold nanoparticles on the structure and neuroprotective function of protein L-isoaspartyl methyltransferase (PIMT)

Abstract Fibrillation of peptides and proteins is implicated in various neurodegenerative diseases and is a global concern. Aging leads to the formation of abnormal isoaspartate (isoAsp) residues from isomerization of normal aspartates in proteins, triggering fibril formation that leads to neurodege...

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Autores principales:	Tanaya Chatterjee, Gaurav Das, Surajit Ghosh, Pinak Chakrabarti
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/da98a0c0a4fc4a1f8ec03f615b3f49c7
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spelling	oai:doaj.org-article:da98a0c0a4fc4a1f8ec03f615b3f49c72021-12-02T15:33:12ZEffect of gold nanoparticles on the structure and neuroprotective function of protein L-isoaspartyl methyltransferase (PIMT)10.1038/s41598-021-93752-12045-2322https://doaj.org/article/da98a0c0a4fc4a1f8ec03f615b3f49c72021-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-93752-1https://doaj.org/toc/2045-2322Abstract Fibrillation of peptides and proteins is implicated in various neurodegenerative diseases and is a global concern. Aging leads to the formation of abnormal isoaspartate (isoAsp) residues from isomerization of normal aspartates in proteins, triggering fibril formation that leads to neurodegenerative diseases. Protein L-isoaspartyl methyltransferase (PIMT) is a repair enzyme which recognizes and converts altered isoAsp residues back to normal aspartate. Here we report the effect of gold nanoparticles (AuNPs) of different sizes on the structure and function of PIMT. Spherical AuNPs, viz. AuNS5, AuNS50 and AuNS100 (the number indicating the diameter in nm) stabilize PIMT, with AuNS100 exhibiting the best efficacy, as evident from various biophysical experiments. Isothermal titration calorimetry (ITC) revealed endothermic, but entropy driven mode of binding of PIMT with all the three AuNSs. Methyltransferase activity assay showed enhanced activity of PIMT in presence of all AuNSs, the maximum being with AuNS100. The efficacy of PIMT in presence of AuNS100 was further demonstrated by the reduction of fibrillation of Aβ42, the peptide that is implicated in Alzheimer’s disease. The enhancement of anti-fibrillation activity of PIMT with AuNS100 was confirmed from cell survival assay with PC12 derived neuronal cells against Aβ42 induced neurotoxicity.Tanaya ChatterjeeGaurav DasSurajit GhoshPinak ChakrabartiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Tanaya Chatterjee Gaurav Das Surajit Ghosh Pinak Chakrabarti Effect of gold nanoparticles on the structure and neuroprotective function of protein L-isoaspartyl methyltransferase (PIMT)
description	Abstract Fibrillation of peptides and proteins is implicated in various neurodegenerative diseases and is a global concern. Aging leads to the formation of abnormal isoaspartate (isoAsp) residues from isomerization of normal aspartates in proteins, triggering fibril formation that leads to neurodegenerative diseases. Protein L-isoaspartyl methyltransferase (PIMT) is a repair enzyme which recognizes and converts altered isoAsp residues back to normal aspartate. Here we report the effect of gold nanoparticles (AuNPs) of different sizes on the structure and function of PIMT. Spherical AuNPs, viz. AuNS5, AuNS50 and AuNS100 (the number indicating the diameter in nm) stabilize PIMT, with AuNS100 exhibiting the best efficacy, as evident from various biophysical experiments. Isothermal titration calorimetry (ITC) revealed endothermic, but entropy driven mode of binding of PIMT with all the three AuNSs. Methyltransferase activity assay showed enhanced activity of PIMT in presence of all AuNSs, the maximum being with AuNS100. The efficacy of PIMT in presence of AuNS100 was further demonstrated by the reduction of fibrillation of Aβ42, the peptide that is implicated in Alzheimer’s disease. The enhancement of anti-fibrillation activity of PIMT with AuNS100 was confirmed from cell survival assay with PC12 derived neuronal cells against Aβ42 induced neurotoxicity.
format	article
author	Tanaya Chatterjee Gaurav Das Surajit Ghosh Pinak Chakrabarti
author_facet	Tanaya Chatterjee Gaurav Das Surajit Ghosh Pinak Chakrabarti
author_sort	Tanaya Chatterjee
title	Effect of gold nanoparticles on the structure and neuroprotective function of protein L-isoaspartyl methyltransferase (PIMT)
title_short	Effect of gold nanoparticles on the structure and neuroprotective function of protein L-isoaspartyl methyltransferase (PIMT)
title_full	Effect of gold nanoparticles on the structure and neuroprotective function of protein L-isoaspartyl methyltransferase (PIMT)
title_fullStr	Effect of gold nanoparticles on the structure and neuroprotective function of protein L-isoaspartyl methyltransferase (PIMT)
title_full_unstemmed	Effect of gold nanoparticles on the structure and neuroprotective function of protein L-isoaspartyl methyltransferase (PIMT)
title_sort	effect of gold nanoparticles on the structure and neuroprotective function of protein l-isoaspartyl methyltransferase (pimt)
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/da98a0c0a4fc4a1f8ec03f615b3f49c7
work_keys_str_mv	AT tanayachatterjee effectofgoldnanoparticlesonthestructureandneuroprotectivefunctionofproteinlisoaspartylmethyltransferasepimt AT gauravdas effectofgoldnanoparticlesonthestructureandneuroprotectivefunctionofproteinlisoaspartylmethyltransferasepimt AT surajitghosh effectofgoldnanoparticlesonthestructureandneuroprotectivefunctionofproteinlisoaspartylmethyltransferasepimt AT pinakchakrabarti effectofgoldnanoparticlesonthestructureandneuroprotectivefunctionofproteinlisoaspartylmethyltransferasepimt
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Effect of gold nanoparticles on the structure and neuroprotective function of protein L-isoaspartyl methyltransferase (PIMT)

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