Dataset of the construction and characterization of stable biological nanoparticles

Autores
Gisonno, Romina Antonela; Tricerri, María Alejandra; González, Marina Cecilia; Garda, Horacio Alberto; Ramella, Nahuel Alberto; Díaz Ludovico, Ivo
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Instituto de Investigaciones Bioquímicas de La Plata
Facultad de Ciencias Médicas
Materia
Ciencias Médicas
Apolipoprotein A-I
BS 3 crosslinker
Lipid-binding
Gradient gel electrophoresis
Nanoparticles
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/125027
Acceder
id SEDICI_87d4e21c24778484e6771c4443ce0010
oai_identifier_str oai:sedici.unlp.edu.ar:10915/125027
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Dataset of the construction and characterization of stable biological nanoparticlesGisonno, Romina AntonelaTricerri, María AlejandraGonzález, Marina CeciliaGarda, Horacio AlbertoRamella, Nahuel AlbertoDíaz Ludovico, IvoCiencias MédicasApolipoprotein A-IBS 3 crosslinkerLipid-bindingGradient gel electrophoresisNanoparticlesThis 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.Instituto de Investigaciones Bioquímicas de La PlataFacultad de Ciencias Médicas2020info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/125027enginfo:eu-repo/semantics/altIdentifier/issn/2352-3409info:eu-repo/semantics/altIdentifier/doi/10.1016/j.dib.2020.106536info:eu-repo/semantics/reference/hdl/10915/125022info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2026-01-14T13:54:25Zoai:sedici.unlp.edu.ar:10915/125027Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292026-01-14 13:54:26.18SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Dataset of the construction and characterization of stable biological nanoparticles
title Dataset of the construction and characterization of stable biological nanoparticles
spellingShingle Dataset of the construction and characterization of stable biological nanoparticles
Gisonno, Romina Antonela
Ciencias Médicas
Apolipoprotein A-I
BS 3 crosslinker
Lipid-binding
Gradient gel electrophoresis
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
dc.creator.none.fl_str_mv Gisonno, Romina Antonela
Tricerri, María Alejandra
González, Marina Cecilia
Garda, Horacio Alberto
Ramella, Nahuel Alberto
Díaz Ludovico, Ivo
author Gisonno, Romina Antonela
author_facet Gisonno, Romina Antonela
Tricerri, María Alejandra
González, Marina Cecilia
Garda, Horacio Alberto
Ramella, Nahuel Alberto
Díaz Ludovico, Ivo
author_role author
author2 Tricerri, María Alejandra
González, Marina Cecilia
Garda, Horacio Alberto
Ramella, Nahuel Alberto
Díaz Ludovico, Ivo
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Ciencias Médicas
Apolipoprotein A-I
BS 3 crosslinker
Lipid-binding
Gradient gel electrophoresis
Nanoparticles
topic Ciencias Médicas
Apolipoprotein A-I
BS 3 crosslinker
Lipid-binding
Gradient gel electrophoresis
Nanoparticles
dc.description.none.fl_txt_mv 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.
Instituto de Investigaciones Bioquímicas de La Plata
Facultad de Ciencias Médicas
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.
publishDate 2020
dc.date.none.fl_str_mv 2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/125027
url http://sedici.unlp.edu.ar/handle/10915/125027
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/2352-3409
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.dib.2020.106536
info:eu-repo/semantics/reference/hdl/10915/125022
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.113929

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