N-terminal mutants of human apolipoprotein A-I : Structural perturbations associated to protein misfolding

Since the early description of different human apolipoprotein A-I variants associated to amyloidosis, the reason that determines its deposition inducing organ failure has been under research. To shed light into the events associated to protein aggregation, we studied the effect of the structural per...

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Autores principales:	Gaddi, Gisela Marina, Gisonno, Romina Antonela, Rosu, Silvana Antonia, Curto, Lucrecia María, Elías, Esteban E., Prieto, Eduardo Daniel, Schinella, Guillermo Raúl, Finarelli, Gabriela Sandra, Cortez, María Fernanda, Ramella, Nahuel Alberto, Tricerri, María Alejandra
Formato:	Articulo Preprint
Lenguaje:	Inglés
Publicado:	2019
Materias:	Ciencias Exactas Química Ciencias Médicas Apolipoprotein A-I variants Organ failure Chronic disease Proteins
Acceso en línea:	http://sedici.unlp.edu.ar/handle/10915/125371
Aporte de:	SEDICI (UNLP) de Universidad Nacional de La Plata

id	I19-R120-10915-125371
record_format	dspace
institution	Universidad Nacional de La Plata
institution_str	I-19
repository_str	R-120
collection	SEDICI (UNLP)
language	Inglés
topic	Ciencias Exactas Química Ciencias Médicas Apolipoprotein A-I variants Organ failure Chronic disease Proteins
spellingShingle	Ciencias Exactas Química Ciencias Médicas Apolipoprotein A-I variants Organ failure Chronic disease Proteins Gaddi, Gisela Marina Gisonno, Romina Antonela Rosu, Silvana Antonia Curto, Lucrecia María Elías, Esteban E. Prieto, Eduardo Daniel Schinella, Guillermo Raúl Finarelli, Gabriela Sandra Cortez, María Fernanda Ramella, Nahuel Alberto Tricerri, María Alejandra N-terminal mutants of human apolipoprotein A-I : Structural perturbations associated to protein misfolding
topic_facet	Ciencias Exactas Química Ciencias Médicas Apolipoprotein A-I variants Organ failure Chronic disease Proteins
description	Since the early description of different human apolipoprotein A-I variants associated to amyloidosis, the reason that determines its deposition inducing organ failure has been under research. To shed light into the events associated to protein aggregation, we studied the effect of the structural perturbations induced by the replacement of a Leucine in position 60 by an Arginine as it occurs in the natural amyloidogenic variant (L60R). Circular dichroism, intrinsic fluorescence measurements and assays of binding to ligands indicate that L60R is more unstable, more sensitive to proteolysis and interacts with sodium dodecyl sulfate (a model of negative lipids) more than the protein with the native sequence and other natural variant tested, involving a replacement of a Trytophan by and Arginine in the amino acid 50 (W50R). In addition, the small structural rearrangement observed under physiological pH leads to the release of tumor necrosis factor α and interleukin-lβ from a model of macrophages. Our results strongly suggest that the chronic disease may be a consequence of the loss in the native conformation which alters the equilibrium among native and cytotoxic proteins conformation.
format	Articulo Preprint
author	Gaddi, Gisela Marina Gisonno, Romina Antonela Rosu, Silvana Antonia Curto, Lucrecia María Elías, Esteban E. Prieto, Eduardo Daniel Schinella, Guillermo Raúl Finarelli, Gabriela Sandra Cortez, María Fernanda Ramella, Nahuel Alberto Tricerri, María Alejandra
author_facet	Gaddi, Gisela Marina Gisonno, Romina Antonela Rosu, Silvana Antonia Curto, Lucrecia María Elías, Esteban E. Prieto, Eduardo Daniel Schinella, Guillermo Raúl Finarelli, Gabriela Sandra Cortez, María Fernanda Ramella, Nahuel Alberto Tricerri, María Alejandra
author_sort	Gaddi, Gisela Marina
title	N-terminal mutants of human apolipoprotein A-I : Structural perturbations associated to protein misfolding
title_short	N-terminal mutants of human apolipoprotein A-I : Structural perturbations associated to protein misfolding
title_full	N-terminal mutants of human apolipoprotein A-I : Structural perturbations associated to protein misfolding
title_fullStr	N-terminal mutants of human apolipoprotein A-I : Structural perturbations associated to protein misfolding
title_full_unstemmed	N-terminal mutants of human apolipoprotein A-I : Structural perturbations associated to protein misfolding
title_sort	n-terminal mutants of human apolipoprotein a-i : structural perturbations associated to protein misfolding
publishDate	2019
url	http://sedici.unlp.edu.ar/handle/10915/125371
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N-terminal mutants of human apolipoprotein A-I : Structural perturbations associated to protein misfolding

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