Global chain properties of an all L-alpha-eicosapeptide with a secondary alpha -helix and its all retro D-inverso-alpha-eicosapeptide estimated through the modeling of their CZE de...

Autores
Deiber, Julio Alcides; Piaggio, María Virginia; Peirotti, Marta Beatriz
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Several global chain properties of relatively long peptides composed of 20 amino acid residues are estimated through the modeling of their experimental effective electrophoretic mobilities determined by CZE for 2 < pH < 6. In this regard, an all L-alpha-eicosapeptide, including a secondary alpha-helix (Peptide 1) and its all retro D-inverso-alpha-eicosapeptide (Peptide 2), are considered. Despite Peptides 1 and 2 are isomeric chains, they do not present similar global conformations in the whole range of pH studied. These peptides may also differ in the quality of BGE components chain interactions depending on the pH value. Three Peptide 1 fragments (Peptides 3, 4, and 5) are also analyzed in this framework with the following purposes: (i) visualization of the effects of initial and final strands at each side of the alpha-helix on the global chain conformations of Peptide 1 at different pHs and (ii) analysis of global chain conformations of Peptides 1 and 2, and Peptide 1 fragments in relation to their pI values. Also, the peptidemaximum andminimum hydrations predicted by the model, compatible with experimental effective electrophoretic mobilities at different pHs, are quantified and discussed, and needs for further research concerning chain hydration are proposed. It is shown that CZE is a useful analytical tool for peptidomimetic designs and purposes.
Fil: Deiber, Julio Alcides. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química (i); Argentina
Fil: Piaggio, María Virginia. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina
Fil: Peirotti, Marta Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química (i); Argentina
Materia
L-Alpha-Eicosapeptide
Peptide Effective Electrophoretic Mobility
Peptide Global Chain Properties
Peptidomimetic Structure-Function
Retro D-Alpha-Peptide
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:11336/9248
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/9248
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Global chain properties of an all L-alpha-eicosapeptide with a secondary alpha -helix and its all retro D-inverso-alpha-eicosapeptide estimated through the modeling of their CZE determined electrophoretic mobilitiesDeiber, Julio AlcidesPiaggio, María VirginiaPeirotti, Marta BeatrizL-Alpha-EicosapeptidePeptide Effective Electrophoretic MobilityPeptide Global Chain PropertiesPeptidomimetic Structure-FunctionRetro D-Alpha-Peptidehttps://purl.org/becyt/ford/2.4https://purl.org/becyt/ford/2Several global chain properties of relatively long peptides composed of 20 amino acid residues are estimated through the modeling of their experimental effective electrophoretic mobilities determined by CZE for 2 < pH < 6. In this regard, an all L-alpha-eicosapeptide, including a secondary alpha-helix (Peptide 1) and its all retro D-inverso-alpha-eicosapeptide (Peptide 2), are considered. Despite Peptides 1 and 2 are isomeric chains, they do not present similar global conformations in the whole range of pH studied. These peptides may also differ in the quality of BGE components chain interactions depending on the pH value. Three Peptide 1 fragments (Peptides 3, 4, and 5) are also analyzed in this framework with the following purposes: (i) visualization of the effects of initial and final strands at each side of the alpha-helix on the global chain conformations of Peptide 1 at different pHs and (ii) analysis of global chain conformations of Peptides 1 and 2, and Peptide 1 fragments in relation to their pI values. Also, the peptidemaximum andminimum hydrations predicted by the model, compatible with experimental effective electrophoretic mobilities at different pHs, are quantified and discussed, and needs for further research concerning chain hydration are proposed. It is shown that CZE is a useful analytical tool for peptidomimetic designs and purposes.Fil: Deiber, Julio Alcides. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química (i); ArgentinaFil: Piaggio, María Virginia. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; ArgentinaFil: Peirotti, Marta Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química (i); ArgentinaWiley2014-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/9248Deiber, Julio Alcides; Piaggio, María Virginia; Peirotti, Marta Beatriz; Global chain properties of an all L-alpha-eicosapeptide with a secondary alpha -helix and its all retro D-inverso-alpha-eicosapeptide estimated through the modeling of their CZE determined electrophoretic mobilities; Wiley; Electrophoresis; 35; 5; 3-2014; 755-7610173-0835enginfo:eu-repo/semantics/altIdentifier/doi/10.1002/elps.201300395info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/elps.201300395/abstractinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:44:37Zoai:ri.conicet.gov.ar:11336/9248instacron: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 09:44:37.41CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Global chain properties of an all L-alpha-eicosapeptide with a secondary alpha -helix and its all retro D-inverso-alpha-eicosapeptide estimated through the modeling of their CZE determined electrophoretic mobilities
title Global chain properties of an all L-alpha-eicosapeptide with a secondary alpha -helix and its all retro D-inverso-alpha-eicosapeptide estimated through the modeling of their CZE determined electrophoretic mobilities
spellingShingle Global chain properties of an all L-alpha-eicosapeptide with a secondary alpha -helix and its all retro D-inverso-alpha-eicosapeptide estimated through the modeling of their CZE determined electrophoretic mobilities
Deiber, Julio Alcides
L-Alpha-Eicosapeptide
Peptide Effective Electrophoretic Mobility
Peptide Global Chain Properties
Peptidomimetic Structure-Function
Retro D-Alpha-Peptide
title_short Global chain properties of an all L-alpha-eicosapeptide with a secondary alpha -helix and its all retro D-inverso-alpha-eicosapeptide estimated through the modeling of their CZE determined electrophoretic mobilities
title_full Global chain properties of an all L-alpha-eicosapeptide with a secondary alpha -helix and its all retro D-inverso-alpha-eicosapeptide estimated through the modeling of their CZE determined electrophoretic mobilities
title_fullStr Global chain properties of an all L-alpha-eicosapeptide with a secondary alpha -helix and its all retro D-inverso-alpha-eicosapeptide estimated through the modeling of their CZE determined electrophoretic mobilities
title_full_unstemmed Global chain properties of an all L-alpha-eicosapeptide with a secondary alpha -helix and its all retro D-inverso-alpha-eicosapeptide estimated through the modeling of their CZE determined electrophoretic mobilities
title_sort Global chain properties of an all L-alpha-eicosapeptide with a secondary alpha -helix and its all retro D-inverso-alpha-eicosapeptide estimated through the modeling of their CZE determined electrophoretic mobilities
dc.creator.none.fl_str_mv Deiber, Julio Alcides
Piaggio, María Virginia
Peirotti, Marta Beatriz
author Deiber, Julio Alcides
author_facet Deiber, Julio Alcides
Piaggio, María Virginia
Peirotti, Marta Beatriz
author_role author
author2 Piaggio, María Virginia
Peirotti, Marta Beatriz
author2_role author
author
dc.subject.none.fl_str_mv L-Alpha-Eicosapeptide
Peptide Effective Electrophoretic Mobility
Peptide Global Chain Properties
Peptidomimetic Structure-Function
Retro D-Alpha-Peptide
topic L-Alpha-Eicosapeptide
Peptide Effective Electrophoretic Mobility
Peptide Global Chain Properties
Peptidomimetic Structure-Function
Retro D-Alpha-Peptide
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Several global chain properties of relatively long peptides composed of 20 amino acid residues are estimated through the modeling of their experimental effective electrophoretic mobilities determined by CZE for 2 < pH < 6. In this regard, an all L-alpha-eicosapeptide, including a secondary alpha-helix (Peptide 1) and its all retro D-inverso-alpha-eicosapeptide (Peptide 2), are considered. Despite Peptides 1 and 2 are isomeric chains, they do not present similar global conformations in the whole range of pH studied. These peptides may also differ in the quality of BGE components chain interactions depending on the pH value. Three Peptide 1 fragments (Peptides 3, 4, and 5) are also analyzed in this framework with the following purposes: (i) visualization of the effects of initial and final strands at each side of the alpha-helix on the global chain conformations of Peptide 1 at different pHs and (ii) analysis of global chain conformations of Peptides 1 and 2, and Peptide 1 fragments in relation to their pI values. Also, the peptidemaximum andminimum hydrations predicted by the model, compatible with experimental effective electrophoretic mobilities at different pHs, are quantified and discussed, and needs for further research concerning chain hydration are proposed. It is shown that CZE is a useful analytical tool for peptidomimetic designs and purposes.
Fil: Deiber, Julio Alcides. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química (i); Argentina
Fil: Piaggio, María Virginia. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina
Fil: Peirotti, Marta Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química (i); Argentina
description Several global chain properties of relatively long peptides composed of 20 amino acid residues are estimated through the modeling of their experimental effective electrophoretic mobilities determined by CZE for 2 < pH < 6. In this regard, an all L-alpha-eicosapeptide, including a secondary alpha-helix (Peptide 1) and its all retro D-inverso-alpha-eicosapeptide (Peptide 2), are considered. Despite Peptides 1 and 2 are isomeric chains, they do not present similar global conformations in the whole range of pH studied. These peptides may also differ in the quality of BGE components chain interactions depending on the pH value. Three Peptide 1 fragments (Peptides 3, 4, and 5) are also analyzed in this framework with the following purposes: (i) visualization of the effects of initial and final strands at each side of the alpha-helix on the global chain conformations of Peptide 1 at different pHs and (ii) analysis of global chain conformations of Peptides 1 and 2, and Peptide 1 fragments in relation to their pI values. Also, the peptidemaximum andminimum hydrations predicted by the model, compatible with experimental effective electrophoretic mobilities at different pHs, are quantified and discussed, and needs for further research concerning chain hydration are proposed. It is shown that CZE is a useful analytical tool for peptidomimetic designs and purposes.
publishDate 2014
dc.date.none.fl_str_mv 2014-03
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/11336/9248
Deiber, Julio Alcides; Piaggio, María Virginia; Peirotti, Marta Beatriz; Global chain properties of an all L-alpha-eicosapeptide with a secondary alpha -helix and its all retro D-inverso-alpha-eicosapeptide estimated through the modeling of their CZE determined electrophoretic mobilities; Wiley; Electrophoresis; 35; 5; 3-2014; 755-761
0173-0835
url http://hdl.handle.net/11336/9248
identifier_str_mv Deiber, Julio Alcides; Piaggio, María Virginia; Peirotti, Marta Beatriz; Global chain properties of an all L-alpha-eicosapeptide with a secondary alpha -helix and its all retro D-inverso-alpha-eicosapeptide estimated through the modeling of their CZE determined electrophoretic mobilities; Wiley; Electrophoresis; 35; 5; 3-2014; 755-761
0173-0835
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1002/elps.201300395
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/elps.201300395/abstract
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
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
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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