Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensity

Autores
Curto, Lucrecia María; Angelani, Carla Romina; Delfino, Jose Maria
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Natural β-folds manage to fold up successfully. By contrast, attempts to dissect fragments or peptides from well folded β-sheet proteins have met with insurmountable difficulties. Here we briefly review selected successful cases of intervention on the well-known scaffold of intestinal fatty acid binding protein (IFABP). Lessons from these examples might set guidelines along the design of proteins belonging to this class. Impact of modifications on topology, binding and aggregation is highlighted. With the aid of abridged variants of IFABP we focus on key structural features responsible for the assembly into oligomeric forms or aggregates.
Fil: Curto, Lucrecia María. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Angelani, Carla Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Delfino, Jose Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Materia
Lipid Binding Proteins
Β-Barrel Protein
Aggregation Propensity
Folding
Intestinal Fatty Acid Binding Protein
Ligand Binding
Amyloid Aggregation
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/17888
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensityCurto, Lucrecia MaríaAngelani, Carla RominaDelfino, Jose MariaLipid Binding ProteinsΒ-Barrel ProteinAggregation PropensityFoldingIntestinal Fatty Acid Binding ProteinLigand BindingAmyloid Aggregationhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Natural β-folds manage to fold up successfully. By contrast, attempts to dissect fragments or peptides from well folded β-sheet proteins have met with insurmountable difficulties. Here we briefly review selected successful cases of intervention on the well-known scaffold of intestinal fatty acid binding protein (IFABP). Lessons from these examples might set guidelines along the design of proteins belonging to this class. Impact of modifications on topology, binding and aggregation is highlighted. With the aid of abridged variants of IFABP we focus on key structural features responsible for the assembly into oligomeric forms or aggregates.Fil: Curto, Lucrecia María. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Angelani, Carla Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Delfino, Jose Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaElsevier2015-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/17888Curto, Lucrecia María; Angelani, Carla Romina; Delfino, Jose Maria; Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensity; Elsevier; Prostaglandins Leukotrienes and Essential Fatty Acids; 93; 2-2015; 37-430952-3278enginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.plefa.2014.08.001info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0952327814001288?via%3Dihubinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:05:01Zoai:ri.conicet.gov.ar:11336/17888instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:05:02.058CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensity
title Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensity
spellingShingle Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensity
Curto, Lucrecia María
Lipid Binding Proteins
Β-Barrel Protein
Aggregation Propensity
Folding
Intestinal Fatty Acid Binding Protein
Ligand Binding
Amyloid Aggregation
title_short Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensity
title_full Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensity
title_fullStr Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensity
title_full_unstemmed Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensity
title_sort Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensity
dc.creator.none.fl_str_mv Curto, Lucrecia María
Angelani, Carla Romina
Delfino, Jose Maria
author Curto, Lucrecia María
author_facet Curto, Lucrecia María
Angelani, Carla Romina
Delfino, Jose Maria
author_role author
author2 Angelani, Carla Romina
Delfino, Jose Maria
author2_role author
author
dc.subject.none.fl_str_mv Lipid Binding Proteins
Β-Barrel Protein
Aggregation Propensity
Folding
Intestinal Fatty Acid Binding Protein
Ligand Binding
Amyloid Aggregation
topic Lipid Binding Proteins
Β-Barrel Protein
Aggregation Propensity
Folding
Intestinal Fatty Acid Binding Protein
Ligand Binding
Amyloid Aggregation
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Natural β-folds manage to fold up successfully. By contrast, attempts to dissect fragments or peptides from well folded β-sheet proteins have met with insurmountable difficulties. Here we briefly review selected successful cases of intervention on the well-known scaffold of intestinal fatty acid binding protein (IFABP). Lessons from these examples might set guidelines along the design of proteins belonging to this class. Impact of modifications on topology, binding and aggregation is highlighted. With the aid of abridged variants of IFABP we focus on key structural features responsible for the assembly into oligomeric forms or aggregates.
Fil: Curto, Lucrecia María. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Angelani, Carla Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Delfino, Jose Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
description Natural β-folds manage to fold up successfully. By contrast, attempts to dissect fragments or peptides from well folded β-sheet proteins have met with insurmountable difficulties. Here we briefly review selected successful cases of intervention on the well-known scaffold of intestinal fatty acid binding protein (IFABP). Lessons from these examples might set guidelines along the design of proteins belonging to this class. Impact of modifications on topology, binding and aggregation is highlighted. With the aid of abridged variants of IFABP we focus on key structural features responsible for the assembly into oligomeric forms or aggregates.
publishDate 2015
dc.date.none.fl_str_mv 2015-02
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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://hdl.handle.net/11336/17888
Curto, Lucrecia María; Angelani, Carla Romina; Delfino, Jose Maria; Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensity; Elsevier; Prostaglandins Leukotrienes and Essential Fatty Acids; 93; 2-2015; 37-43
0952-3278
url http://hdl.handle.net/11336/17888
identifier_str_mv Curto, Lucrecia María; Angelani, Carla Romina; Delfino, Jose Maria; Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensity; Elsevier; Prostaglandins Leukotrienes and Essential Fatty Acids; 93; 2-2015; 37-43
0952-3278
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.plefa.2014.08.001
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0952327814001288?via%3Dihub
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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