Structure and interactions of fish type III antifreeze protein in solution

Autores
Salvay, Andrés Gerardo; Gabel, Frank; Pucci, Bernard; Santos, Javier; Howards, Eduardo I.; Ebel, Christine
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
It has been suggested that above a critical protein concentration, fish Type III antifreeze protein (AFP III) selfassembles to form micelle-like structures that may play a key role In antifreeze activity. To understand the complex activity of AFP III, a comprehensive description of its association state and structural organization in solution is necessary. We used analytical ultracentrifugation, analytical size-exclusion chromatography, and dynamic light scattering to characterize the interactions and homogeneity of AFP III in solution. Small-angle neutron scattering was used to determine the low-resolution structure in solution. Our results clearly show that at concentrations up to 20 mg mL-1 and at temperatures of 20°C, 6°C, and 4°C, AFP III is monomeric in solution and adopts a structure compatible with that determined by crystallography. Surface tension measurements show a propensity of AFP III to localize at the air/water interface, but this surface activity is not correlated with any aggregation in the bulk. These results support the hypothesis that each AFP III molecule acts independently of the others, and that specific intermolecular interactions between monomers are not required for binding to ice. The lack of attractive interactions between monomers may be functionally important, allowing for more efficient binding and covering of the ice surface.
Fil: Salvay, Andrés Gerardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina
Fil: Gabel, Frank. Commissariat A Energie Atomique; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Pucci, Bernard. Université D'avignon Et Des Pays Du Vaucluse; Francia
Fil: Santos, Javier. 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: Howards, Eduardo I.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina
Fil: Ebel, Christine. Commissariat A Energie Atomique; Francia. Centre National de la Recherche Scientifique; Francia
Materia
Antifreeze proteins
AFP III
protein interactions
Structure in solution
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/198526
Acceder
id CONICETDig_2db11ce9b98de3d172b5c511a9a16095
oai_identifier_str oai:ri.conicet.gov.ar:11336/198526
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Structure and interactions of fish type III antifreeze protein in solutionSalvay, Andrés GerardoGabel, FrankPucci, BernardSantos, JavierHowards, Eduardo I.Ebel, ChristineAntifreeze proteinsAFP IIIprotein interactionsStructure in solutionhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.3https://purl.org/becyt/ford/1It has been suggested that above a critical protein concentration, fish Type III antifreeze protein (AFP III) selfassembles to form micelle-like structures that may play a key role In antifreeze activity. To understand the complex activity of AFP III, a comprehensive description of its association state and structural organization in solution is necessary. We used analytical ultracentrifugation, analytical size-exclusion chromatography, and dynamic light scattering to characterize the interactions and homogeneity of AFP III in solution. Small-angle neutron scattering was used to determine the low-resolution structure in solution. Our results clearly show that at concentrations up to 20 mg mL-1 and at temperatures of 20°C, 6°C, and 4°C, AFP III is monomeric in solution and adopts a structure compatible with that determined by crystallography. Surface tension measurements show a propensity of AFP III to localize at the air/water interface, but this surface activity is not correlated with any aggregation in the bulk. These results support the hypothesis that each AFP III molecule acts independently of the others, and that specific intermolecular interactions between monomers are not required for binding to ice. The lack of attractive interactions between monomers may be functionally important, allowing for more efficient binding and covering of the ice surface.Fil: Salvay, Andrés Gerardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; ArgentinaFil: Gabel, Frank. Commissariat A Energie Atomique; Francia. Centre National de la Recherche Scientifique; FranciaFil: Pucci, Bernard. Université D'avignon Et Des Pays Du Vaucluse; FranciaFil: Santos, Javier. 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: Howards, Eduardo I.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; ArgentinaFil: Ebel, Christine. Commissariat A Energie Atomique; Francia. Centre National de la Recherche Scientifique; FranciaCell Press2010-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/198526Salvay, Andrés Gerardo; Gabel, Frank; Pucci, Bernard; Santos, Javier; Howards, Eduardo I.; et al.; Structure and interactions of fish type III antifreeze protein in solution; Cell Press; Biophysical Journal; 99; 2; 7-2010; 609-6180006-3495CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.cell.com/biophysj/retrieve/pii/S000634951000528Xinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpj.2010.04.030info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:36:55Zoai:ri.conicet.gov.ar:11336/198526instacron: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:34982025-09-29 09:36:55.306CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Structure and interactions of fish type III antifreeze protein in solution
title Structure and interactions of fish type III antifreeze protein in solution
spellingShingle Structure and interactions of fish type III antifreeze protein in solution
Salvay, Andrés Gerardo
Antifreeze proteins
AFP III
protein interactions
Structure in solution
title_short Structure and interactions of fish type III antifreeze protein in solution
title_full Structure and interactions of fish type III antifreeze protein in solution
title_fullStr Structure and interactions of fish type III antifreeze protein in solution
title_full_unstemmed Structure and interactions of fish type III antifreeze protein in solution
title_sort Structure and interactions of fish type III antifreeze protein in solution
dc.creator.none.fl_str_mv Salvay, Andrés Gerardo
Gabel, Frank
Pucci, Bernard
Santos, Javier
Howards, Eduardo I.
Ebel, Christine
author Salvay, Andrés Gerardo
author_facet Salvay, Andrés Gerardo
Gabel, Frank
Pucci, Bernard
Santos, Javier
Howards, Eduardo I.
Ebel, Christine
author_role author
author2 Gabel, Frank
Pucci, Bernard
Santos, Javier
Howards, Eduardo I.
Ebel, Christine
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Antifreeze proteins
AFP III
protein interactions
Structure in solution
topic Antifreeze proteins
AFP III
protein interactions
Structure in solution
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/1.3
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv It has been suggested that above a critical protein concentration, fish Type III antifreeze protein (AFP III) selfassembles to form micelle-like structures that may play a key role In antifreeze activity. To understand the complex activity of AFP III, a comprehensive description of its association state and structural organization in solution is necessary. We used analytical ultracentrifugation, analytical size-exclusion chromatography, and dynamic light scattering to characterize the interactions and homogeneity of AFP III in solution. Small-angle neutron scattering was used to determine the low-resolution structure in solution. Our results clearly show that at concentrations up to 20 mg mL-1 and at temperatures of 20°C, 6°C, and 4°C, AFP III is monomeric in solution and adopts a structure compatible with that determined by crystallography. Surface tension measurements show a propensity of AFP III to localize at the air/water interface, but this surface activity is not correlated with any aggregation in the bulk. These results support the hypothesis that each AFP III molecule acts independently of the others, and that specific intermolecular interactions between monomers are not required for binding to ice. The lack of attractive interactions between monomers may be functionally important, allowing for more efficient binding and covering of the ice surface.
Fil: Salvay, Andrés Gerardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina
Fil: Gabel, Frank. Commissariat A Energie Atomique; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Pucci, Bernard. Université D'avignon Et Des Pays Du Vaucluse; Francia
Fil: Santos, Javier. 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: Howards, Eduardo I.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina
Fil: Ebel, Christine. Commissariat A Energie Atomique; Francia. Centre National de la Recherche Scientifique; Francia
description It has been suggested that above a critical protein concentration, fish Type III antifreeze protein (AFP III) selfassembles to form micelle-like structures that may play a key role In antifreeze activity. To understand the complex activity of AFP III, a comprehensive description of its association state and structural organization in solution is necessary. We used analytical ultracentrifugation, analytical size-exclusion chromatography, and dynamic light scattering to characterize the interactions and homogeneity of AFP III in solution. Small-angle neutron scattering was used to determine the low-resolution structure in solution. Our results clearly show that at concentrations up to 20 mg mL-1 and at temperatures of 20°C, 6°C, and 4°C, AFP III is monomeric in solution and adopts a structure compatible with that determined by crystallography. Surface tension measurements show a propensity of AFP III to localize at the air/water interface, but this surface activity is not correlated with any aggregation in the bulk. These results support the hypothesis that each AFP III molecule acts independently of the others, and that specific intermolecular interactions between monomers are not required for binding to ice. The lack of attractive interactions between monomers may be functionally important, allowing for more efficient binding and covering of the ice surface.
publishDate 2010
dc.date.none.fl_str_mv 2010-07
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/11336/198526
Salvay, Andrés Gerardo; Gabel, Frank; Pucci, Bernard; Santos, Javier; Howards, Eduardo I.; et al.; Structure and interactions of fish type III antifreeze protein in solution; Cell Press; Biophysical Journal; 99; 2; 7-2010; 609-618
0006-3495
CONICET Digital
CONICET
url http://hdl.handle.net/11336/198526
identifier_str_mv Salvay, Andrés Gerardo; Gabel, Frank; Pucci, Bernard; Santos, Javier; Howards, Eduardo I.; et al.; Structure and interactions of fish type III antifreeze protein in solution; Cell Press; Biophysical Journal; 99; 2; 7-2010; 609-618
0006-3495
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.cell.com/biophysj/retrieve/pii/S000634951000528X
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpj.2010.04.030
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Cell Press
publisher.none.fl_str_mv Cell Press
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 13.070432

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