Dataset of the construction and characterization of stable biological nanoparticles

This article shows the dataset of clearance assays and the reconstitution of stable biological nano-complexes using both detergent-assisted and spontaneous solubilization of phospholipids by the recombinant purified apolipoprotein A-I (apoA-I). Protein was intra-chain crosslinked in order to introdu...

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Autores principales: Gisonno, Romina Antonela, Tricerri, María Alejandra, González, Marina Cecilia, Garda, Horacio Alberto, Ramella, Nahuel Alberto, Díaz Ludovico, Ivo
Formato: Articulo
Lenguaje:Inglés
Publicado: 2020
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Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/125027
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id I19-R120-10915-125027
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Médicas
Apolipoprotein A-I
BS 3 crosslinker
Lipid-binding
Gradient gel electrophoresis
Nanoparticles
spellingShingle Ciencias Médicas
Apolipoprotein A-I
BS 3 crosslinker
Lipid-binding
Gradient gel electrophoresis
Nanoparticles
Gisonno, Romina Antonela
Tricerri, María Alejandra
González, Marina Cecilia
Garda, Horacio Alberto
Ramella, Nahuel Alberto
Díaz Ludovico, Ivo
Dataset of the construction and characterization of stable biological nanoparticles
topic_facet Ciencias Médicas
Apolipoprotein A-I
BS 3 crosslinker
Lipid-binding
Gradient gel electrophoresis
Nanoparticles
description This article shows the dataset of clearance assays and the reconstitution of stable biological nano-complexes using both detergent-assisted and spontaneous solubilization of phospholipids by the recombinant purified apolipoprotein A-I (apoA-I). Protein was intra-chain crosslinked in order to introduce steric constrains. Then, native and crosslinked protein function was evaluated by a data collection of dimiristoyl phosphatidyl choline (DMPC) micellization curves. Additionally, resulting particles from spontaneous or detergent-assisted lipid solubilization were characterized by transmission electron microscopy (TEM), size exclusion chromatog-raphy (SEC), and native polyacrylamide gel electrophoresis (PAGE). Here we set up an experimental design that may help study protein structure based on its function, since interaction with biological membranes and lipids is an intrinsic activity attributed to many proteins in circulation. In addition, by t-test analysis of collected-data, we examined the formation of lipoprotein particles by native and intra-chain crosslinked proteins under different conditions like temperature and time incubation. Thus, data shown here strengthen the usefulness of an easy, rapid, accessible and inexpensive approach to test protein flexibility related to its function.
format Articulo
Articulo
author Gisonno, Romina Antonela
Tricerri, María Alejandra
González, Marina Cecilia
Garda, Horacio Alberto
Ramella, Nahuel Alberto
Díaz Ludovico, Ivo
author_facet Gisonno, Romina Antonela
Tricerri, María Alejandra
González, Marina Cecilia
Garda, Horacio Alberto
Ramella, Nahuel Alberto
Díaz Ludovico, Ivo
author_sort Gisonno, Romina Antonela
title Dataset of the construction and characterization of stable biological nanoparticles
title_short Dataset of the construction and characterization of stable biological nanoparticles
title_full Dataset of the construction and characterization of stable biological nanoparticles
title_fullStr Dataset of the construction and characterization of stable biological nanoparticles
title_full_unstemmed Dataset of the construction and characterization of stable biological nanoparticles
title_sort dataset of the construction and characterization of stable biological nanoparticles
publishDate 2020
url http://sedici.unlp.edu.ar/handle/10915/125027
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