Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant

The article shows dataset of the proteolysis of a natural variant of apolipoprotein A-I (apoA-I) with a substitution of a leucine by and arginine in position 60 (L60R), in comparison with the protein with the native sequence (Wt). This information demonstrates the potential of in vitro partial prote...

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Autores principales:	Gaddi, Gisela Marina, Gisonno, Romina Antonela, Rosu, Silvana Antonia, Cortez, María Fernanda, Finarelli, Gabriela Sandra, Ramella, Nahuel Alberto, Tricerri, María Alejandra
Formato:	Articulo
Lenguaje:	Inglés
Publicado:	2020
Materias:	Química Ciencias Médicas Apolipoprotein A-I -partial proteolysis Analysis-protein structure Catabolism-protein flexibility
Acceso en línea:	http://sedici.unlp.edu.ar/handle/10915/107733 http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC7352074&blobtype=pdf
Aporte de:	SEDICI (UNLP) de Universidad Nacional de La Plata

id	I19-R120-10915-107733
record_format	dspace
institution	Universidad Nacional de La Plata
institution_str	I-19
repository_str	R-120
collection	SEDICI (UNLP)
language	Inglés
topic	Química Ciencias Médicas Apolipoprotein A-I -partial proteolysis Analysis-protein structure Catabolism-protein flexibility
spellingShingle	Química Ciencias Médicas Apolipoprotein A-I -partial proteolysis Analysis-protein structure Catabolism-protein flexibility Gaddi, Gisela Marina Gisonno, Romina Antonela Rosu, Silvana Antonia Cortez, María Fernanda Finarelli, Gabriela Sandra Ramella, Nahuel Alberto Tricerri, María Alejandra Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant
topic_facet	Química Ciencias Médicas Apolipoprotein A-I -partial proteolysis Analysis-protein structure Catabolism-protein flexibility
description	The article shows dataset of the proteolysis of a natural variant of apolipoprotein A-I (apoA-I) with a substitution of a leucine by and arginine in position 60 (L60R), in comparison with the protein with the native sequence (Wt). This information demonstrates the potential of in vitro partial proteolysis experiments as it may be applicable to different approaches in the biophysical field. We have analyzed by different electrophoresis techniques apoA-I variants, quantified the degree of proteolysis after staining and compared the proteolysis efficiency with the computed cleavage patterns. The data shown here clearly strengthen the usefulness of this approach to test protein flexibility, as it may be attained with enzymes which are not expected to modify in vivo this protein but have a well-known digestion pattern. In addition it is appropriate for evaluating protein catabolism, as it is exemplified here by the evidence with metalloproteinase 12 (MMP-12), which is a physiological protease that may elicit the pro-inflammatory processing of this variant within the lesions. We support the work “Structural analysis of a natural apolipoprotein A-I variant (L60R) associated with amyloidosis” (Gaddi, et al., 2020), gaining insights on protein folding from a characterization by proteolysis analysis.
format	Articulo Articulo
author	Gaddi, Gisela Marina Gisonno, Romina Antonela Rosu, Silvana Antonia Cortez, María Fernanda Finarelli, Gabriela Sandra Ramella, Nahuel Alberto Tricerri, María Alejandra
author_facet	Gaddi, Gisela Marina Gisonno, Romina Antonela Rosu, Silvana Antonia Cortez, María Fernanda Finarelli, Gabriela Sandra Ramella, Nahuel Alberto Tricerri, María Alejandra
author_sort	Gaddi, Gisela Marina
title	Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant
title_short	Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant
title_full	Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant
title_fullStr	Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant
title_full_unstemmed	Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant
title_sort	data regarding the sensibility to proteolysis of a natural apolipoprotein a-i mutant
publishDate	2020
url	http://sedici.unlp.edu.ar/handle/10915/107733 http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC7352074&blobtype=pdf
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Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant

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