Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal Interaction

Autores
Mobili, Pablo; Serradell, María de los Ángeles; Mayer, Claudine; Arluison, Véronique; Gómez Zavaglia, Andrea
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Surface-layers (S-layers) are macromolecular paracrystalline arrays of proteins or glycoproteins that can self-assemble into 2-dimensional semi-permeable meshworks to overlay the cell surface of many bacteria and archaea. They usually assemble into lattices with oblique, square or hexagonal symmetry and serve as an interface between the bacterial cell and the environment. Isolated S-layers can recrystallize into two-dimensional regular arrays in suspension or on various surfaces, thus being an appropriate material for several bionanotechnological purposes. Promising applications of S-layers include their use as biotemplates for the capture of metal ions or the synthesis of metal nanoclusters. Considering the use of S-layers as biotemplates for the organization of metal ions or metallic nanoclusters, research on potential of surface layer proteins (SLP) and metals can be understood as an interdisciplinary field, in which different biophysical techniques supply complementary information. In this review, we discuss the SLP as native or engineered “bottom-up” building blocks for metal immobilization structures. We also describe the biophysical techniques used to analyze metal binding properties as well as the information obtained from the investigation of these structures.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
Facultad de Ciencias Exactas
Materia
Bioquímica
Protein-self-assembly
Metal-ions biosorption
Biomineralization
Nanobiotechnology
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/102454
Acceder
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repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal InteractionMobili, PabloSerradell, María de los ÁngelesMayer, ClaudineArluison, VéroniqueGómez Zavaglia, AndreaBioquímicaProtein-self-assemblyMetal-ions biosorptionBiomineralizationNanobiotechnologySurface-layers (S-layers) are macromolecular paracrystalline arrays of proteins or glycoproteins that can self-assemble into 2-dimensional semi-permeable meshworks to overlay the cell surface of many bacteria and archaea. They usually assemble into lattices with oblique, square or hexagonal symmetry and serve as an interface between the bacterial cell and the environment. Isolated S-layers can recrystallize into two-dimensional regular arrays in suspension or on various surfaces, thus being an appropriate material for several bionanotechnological purposes. Promising applications of S-layers include their use as biotemplates for the capture of metal ions or the synthesis of metal nanoclusters. Considering the use of S-layers as biotemplates for the organization of metal ions or metallic nanoclusters, research on potential of surface layer proteins (SLP) and metals can be understood as an interdisciplinary field, in which different biophysical techniques supply complementary information. In this review, we discuss the SLP as native or engineered “bottom-up” building blocks for metal immobilization structures. We also describe the biophysical techniques used to analyze metal binding properties as well as the information obtained from the investigation of these structures.Centro de Investigación y Desarrollo en Criotecnología de AlimentosFacultad de Ciencias Exactas2013-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf39-62http://sedici.unlp.edu.ar/handle/10915/102454enginfo:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/10645info:eu-repo/semantics/altIdentifier/issn/2231-086Xinfo:eu-repo/semantics/altIdentifier/doi/10.9734/IJBCRR/2013/2431info:eu-repo/semantics/altIdentifier/hdl/11336/10645info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2026-03-31T12:08:50Zoai:sedici.unlp.edu.ar:10915/102454Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292026-03-31 12:08:50.6SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal Interaction
title Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal Interaction
spellingShingle Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal Interaction
Mobili, Pablo
Bioquímica
Protein-self-assembly
Metal-ions biosorption
Biomineralization
Nanobiotechnology
title_short Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal Interaction
title_full Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal Interaction
title_fullStr Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal Interaction
title_full_unstemmed Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal Interaction
title_sort Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal Interaction
dc.creator.none.fl_str_mv Mobili, Pablo
Serradell, María de los Ángeles
Mayer, Claudine
Arluison, Véronique
Gómez Zavaglia, Andrea
author Mobili, Pablo
author_facet Mobili, Pablo
Serradell, María de los Ángeles
Mayer, Claudine
Arluison, Véronique
Gómez Zavaglia, Andrea
author_role author
author2 Serradell, María de los Ángeles
Mayer, Claudine
Arluison, Véronique
Gómez Zavaglia, Andrea
author2_role author
author
author
author
dc.subject.none.fl_str_mv Bioquímica
Protein-self-assembly
Metal-ions biosorption
Biomineralization
Nanobiotechnology
topic Bioquímica
Protein-self-assembly
Metal-ions biosorption
Biomineralization
Nanobiotechnology
dc.description.none.fl_txt_mv Surface-layers (S-layers) are macromolecular paracrystalline arrays of proteins or glycoproteins that can self-assemble into 2-dimensional semi-permeable meshworks to overlay the cell surface of many bacteria and archaea. They usually assemble into lattices with oblique, square or hexagonal symmetry and serve as an interface between the bacterial cell and the environment. Isolated S-layers can recrystallize into two-dimensional regular arrays in suspension or on various surfaces, thus being an appropriate material for several bionanotechnological purposes. Promising applications of S-layers include their use as biotemplates for the capture of metal ions or the synthesis of metal nanoclusters. Considering the use of S-layers as biotemplates for the organization of metal ions or metallic nanoclusters, research on potential of surface layer proteins (SLP) and metals can be understood as an interdisciplinary field, in which different biophysical techniques supply complementary information. In this review, we discuss the SLP as native or engineered “bottom-up” building blocks for metal immobilization structures. We also describe the biophysical techniques used to analyze metal binding properties as well as the information obtained from the investigation of these structures.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
Facultad de Ciencias Exactas
description Surface-layers (S-layers) are macromolecular paracrystalline arrays of proteins or glycoproteins that can self-assemble into 2-dimensional semi-permeable meshworks to overlay the cell surface of many bacteria and archaea. They usually assemble into lattices with oblique, square or hexagonal symmetry and serve as an interface between the bacterial cell and the environment. Isolated S-layers can recrystallize into two-dimensional regular arrays in suspension or on various surfaces, thus being an appropriate material for several bionanotechnological purposes. Promising applications of S-layers include their use as biotemplates for the capture of metal ions or the synthesis of metal nanoclusters. Considering the use of S-layers as biotemplates for the organization of metal ions or metallic nanoclusters, research on potential of surface layer proteins (SLP) and metals can be understood as an interdisciplinary field, in which different biophysical techniques supply complementary information. In this review, we discuss the SLP as native or engineered “bottom-up” building blocks for metal immobilization structures. We also describe the biophysical techniques used to analyze metal binding properties as well as the information obtained from the investigation of these structures.
publishDate 2013
dc.date.none.fl_str_mv 2013-02
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/10915/102454
url http://sedici.unlp.edu.ar/handle/10915/102454
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/10645
info:eu-repo/semantics/altIdentifier/issn/2231-086X
info:eu-repo/semantics/altIdentifier/doi/10.9734/IJBCRR/2013/2431
info:eu-repo/semantics/altIdentifier/hdl/11336/10645
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
39-62
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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