Chemometrics: An important tool for monitoring interactions of vitamin B7 with bovine serum albumin with the aim of developing an efficient biosensing system for the analysis of pr...

Autores
Gholivand, Mohammad Bagher; Jalalvand, Ali R.; Goicoechea, Hector Casimiro; Gargallo, Raimundo; Skov, Thomas
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
For the first time, interaction of vitamin B7 (VB7) with bovine serum albumin (BSA) was investigated with the aim of developing a method for the analysis of BSA. The interaction of VB7 with BSA was investigated by cyclic voltammetry (CV), linear sweep voltammetry (LSV), and differential pulse voltammetry (DPV) at a multi-walled carbon nanotubes-modified glassy carbon electrode (MWCNTs/GCE). The recorded electrochemical data was combined with UVvis and fluorescence (F) spectroscopic data into a row- and column-wise augmented matrix and resolved by multivariate curve resolution-alternating least squares (MCR-ALS) as an efficient chemometric tool, and this assisted in the further elucidation of the above interaction. Also, with aid of MCR-BANDS method, the absence of rotational ambiguity was verified in the obtained results and we confirmed that the obtained results were unambiguous and reliable. The binding of VB7 to BSA was also modeled by molecular docking methods. Excellent agreement was found between the experimental and computational results. The differences of DPV responses of VB7 in the absence and presence of BSA (ΔI) were found to be linearly related to BSA concentration between 0.5×10-9 mol L-1 and 35.0×10-9 mol L-1, and a limit of detection (LOD, 3Sb/b) of 0.22×10-9 mol L-1 was calculated. Finally, the DPV method was further applied to the determination of serum albumin (SA) in serum samples obtained from Holstein cows and the results were in good agreement with those obtained by a medical diagnostic laboratory whose method was based on traditional cellulose acetate electrophoresis. The MWCNTs/GCE showed enhanced electron transfer kinetics, large electroactive surface area, and was highly sensitive, selective, and stable towards SA determination. The satisfactory analytical performance of the proposed method would make it potentially advantageous for a broad range of biosensing and clinical applications
Fil: Gholivand, Mohammad Bagher. Razi University. Faculty of Chemistry; Irán
Fil: Jalalvand, Ali R.. Razi University. Faculty of Chemistry; Irán. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Laboratorio de Química Analitica; Argentina
Fil: Goicoechea, Hector Casimiro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Laboratorio de Química Analitica; Argentina
Fil: Gargallo, Raimundo. Universidad de Barcelona; España
Fil: Skov, Thomas. Universidad de Copenhagen; Dinamarca
Materia
Vitamin B7
Bovine Serum Albumin
Binding
Chemometrics
Protein Analysis
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:11336/17015
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/17015
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Chemometrics: An important tool for monitoring interactions of vitamin B7 with bovine serum albumin with the aim of developing an efficient biosensing system for the analysis of proteinGholivand, Mohammad BagherJalalvand, Ali R.Goicoechea, Hector CasimiroGargallo, RaimundoSkov, ThomasVitamin B7Bovine Serum AlbuminBindingChemometricsProtein Analysishttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1For the first time, interaction of vitamin B7 (VB7) with bovine serum albumin (BSA) was investigated with the aim of developing a method for the analysis of BSA. The interaction of VB7 with BSA was investigated by cyclic voltammetry (CV), linear sweep voltammetry (LSV), and differential pulse voltammetry (DPV) at a multi-walled carbon nanotubes-modified glassy carbon electrode (MWCNTs/GCE). The recorded electrochemical data was combined with UVvis and fluorescence (F) spectroscopic data into a row- and column-wise augmented matrix and resolved by multivariate curve resolution-alternating least squares (MCR-ALS) as an efficient chemometric tool, and this assisted in the further elucidation of the above interaction. Also, with aid of MCR-BANDS method, the absence of rotational ambiguity was verified in the obtained results and we confirmed that the obtained results were unambiguous and reliable. The binding of VB7 to BSA was also modeled by molecular docking methods. Excellent agreement was found between the experimental and computational results. The differences of DPV responses of VB7 in the absence and presence of BSA (ΔI) were found to be linearly related to BSA concentration between 0.5×10-9 mol L-1 and 35.0×10-9 mol L-1, and a limit of detection (LOD, 3Sb/b) of 0.22×10-9 mol L-1 was calculated. Finally, the DPV method was further applied to the determination of serum albumin (SA) in serum samples obtained from Holstein cows and the results were in good agreement with those obtained by a medical diagnostic laboratory whose method was based on traditional cellulose acetate electrophoresis. The MWCNTs/GCE showed enhanced electron transfer kinetics, large electroactive surface area, and was highly sensitive, selective, and stable towards SA determination. The satisfactory analytical performance of the proposed method would make it potentially advantageous for a broad range of biosensing and clinical applicationsFil: Gholivand, Mohammad Bagher. Razi University. Faculty of Chemistry; IránFil: Jalalvand, Ali R.. Razi University. Faculty of Chemistry; Irán. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Laboratorio de Química Analitica; ArgentinaFil: Goicoechea, Hector Casimiro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Laboratorio de Química Analitica; ArgentinaFil: Gargallo, Raimundo. Universidad de Barcelona; EspañaFil: Skov, Thomas. Universidad de Copenhagen; DinamarcaElsevier2015-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/17015Gholivand, Mohammad Bagher; Jalalvand, Ali R.; Goicoechea, Hector Casimiro; Gargallo, Raimundo; Skov, Thomas; Chemometrics: An important tool for monitoring interactions of vitamin B7 with bovine serum albumin with the aim of developing an efficient biosensing system for the analysis of protein; Elsevier; Talanta; 132; 1-2015; 354-3650039-9140enginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.talanta.2014.09.019info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0039914014007851info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:03:22Zoai:ri.conicet.gov.ar:11336/17015instacron: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 10:03:23.196CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Chemometrics: An important tool for monitoring interactions of vitamin B7 with bovine serum albumin with the aim of developing an efficient biosensing system for the analysis of protein
title Chemometrics: An important tool for monitoring interactions of vitamin B7 with bovine serum albumin with the aim of developing an efficient biosensing system for the analysis of protein
spellingShingle Chemometrics: An important tool for monitoring interactions of vitamin B7 with bovine serum albumin with the aim of developing an efficient biosensing system for the analysis of protein
Gholivand, Mohammad Bagher
Vitamin B7
Bovine Serum Albumin
Binding
Chemometrics
Protein Analysis
title_short Chemometrics: An important tool for monitoring interactions of vitamin B7 with bovine serum albumin with the aim of developing an efficient biosensing system for the analysis of protein
title_full Chemometrics: An important tool for monitoring interactions of vitamin B7 with bovine serum albumin with the aim of developing an efficient biosensing system for the analysis of protein
title_fullStr Chemometrics: An important tool for monitoring interactions of vitamin B7 with bovine serum albumin with the aim of developing an efficient biosensing system for the analysis of protein
title_full_unstemmed Chemometrics: An important tool for monitoring interactions of vitamin B7 with bovine serum albumin with the aim of developing an efficient biosensing system for the analysis of protein
title_sort Chemometrics: An important tool for monitoring interactions of vitamin B7 with bovine serum albumin with the aim of developing an efficient biosensing system for the analysis of protein
dc.creator.none.fl_str_mv Gholivand, Mohammad Bagher
Jalalvand, Ali R.
Goicoechea, Hector Casimiro
Gargallo, Raimundo
Skov, Thomas
author Gholivand, Mohammad Bagher
author_facet Gholivand, Mohammad Bagher
Jalalvand, Ali R.
Goicoechea, Hector Casimiro
Gargallo, Raimundo
Skov, Thomas
author_role author
author2 Jalalvand, Ali R.
Goicoechea, Hector Casimiro
Gargallo, Raimundo
Skov, Thomas
author2_role author
author
author
author
dc.subject.none.fl_str_mv Vitamin B7
Bovine Serum Albumin
Binding
Chemometrics
Protein Analysis
topic Vitamin B7
Bovine Serum Albumin
Binding
Chemometrics
Protein Analysis
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv For the first time, interaction of vitamin B7 (VB7) with bovine serum albumin (BSA) was investigated with the aim of developing a method for the analysis of BSA. The interaction of VB7 with BSA was investigated by cyclic voltammetry (CV), linear sweep voltammetry (LSV), and differential pulse voltammetry (DPV) at a multi-walled carbon nanotubes-modified glassy carbon electrode (MWCNTs/GCE). The recorded electrochemical data was combined with UVvis and fluorescence (F) spectroscopic data into a row- and column-wise augmented matrix and resolved by multivariate curve resolution-alternating least squares (MCR-ALS) as an efficient chemometric tool, and this assisted in the further elucidation of the above interaction. Also, with aid of MCR-BANDS method, the absence of rotational ambiguity was verified in the obtained results and we confirmed that the obtained results were unambiguous and reliable. The binding of VB7 to BSA was also modeled by molecular docking methods. Excellent agreement was found between the experimental and computational results. The differences of DPV responses of VB7 in the absence and presence of BSA (ΔI) were found to be linearly related to BSA concentration between 0.5×10-9 mol L-1 and 35.0×10-9 mol L-1, and a limit of detection (LOD, 3Sb/b) of 0.22×10-9 mol L-1 was calculated. Finally, the DPV method was further applied to the determination of serum albumin (SA) in serum samples obtained from Holstein cows and the results were in good agreement with those obtained by a medical diagnostic laboratory whose method was based on traditional cellulose acetate electrophoresis. The MWCNTs/GCE showed enhanced electron transfer kinetics, large electroactive surface area, and was highly sensitive, selective, and stable towards SA determination. The satisfactory analytical performance of the proposed method would make it potentially advantageous for a broad range of biosensing and clinical applications
Fil: Gholivand, Mohammad Bagher. Razi University. Faculty of Chemistry; Irán
Fil: Jalalvand, Ali R.. Razi University. Faculty of Chemistry; Irán. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Laboratorio de Química Analitica; Argentina
Fil: Goicoechea, Hector Casimiro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Laboratorio de Química Analitica; Argentina
Fil: Gargallo, Raimundo. Universidad de Barcelona; España
Fil: Skov, Thomas. Universidad de Copenhagen; Dinamarca
description For the first time, interaction of vitamin B7 (VB7) with bovine serum albumin (BSA) was investigated with the aim of developing a method for the analysis of BSA. The interaction of VB7 with BSA was investigated by cyclic voltammetry (CV), linear sweep voltammetry (LSV), and differential pulse voltammetry (DPV) at a multi-walled carbon nanotubes-modified glassy carbon electrode (MWCNTs/GCE). The recorded electrochemical data was combined with UVvis and fluorescence (F) spectroscopic data into a row- and column-wise augmented matrix and resolved by multivariate curve resolution-alternating least squares (MCR-ALS) as an efficient chemometric tool, and this assisted in the further elucidation of the above interaction. Also, with aid of MCR-BANDS method, the absence of rotational ambiguity was verified in the obtained results and we confirmed that the obtained results were unambiguous and reliable. The binding of VB7 to BSA was also modeled by molecular docking methods. Excellent agreement was found between the experimental and computational results. The differences of DPV responses of VB7 in the absence and presence of BSA (ΔI) were found to be linearly related to BSA concentration between 0.5×10-9 mol L-1 and 35.0×10-9 mol L-1, and a limit of detection (LOD, 3Sb/b) of 0.22×10-9 mol L-1 was calculated. Finally, the DPV method was further applied to the determination of serum albumin (SA) in serum samples obtained from Holstein cows and the results were in good agreement with those obtained by a medical diagnostic laboratory whose method was based on traditional cellulose acetate electrophoresis. The MWCNTs/GCE showed enhanced electron transfer kinetics, large electroactive surface area, and was highly sensitive, selective, and stable towards SA determination. The satisfactory analytical performance of the proposed method would make it potentially advantageous for a broad range of biosensing and clinical applications
publishDate 2015
dc.date.none.fl_str_mv 2015-01
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/11336/17015
Gholivand, Mohammad Bagher; Jalalvand, Ali R.; Goicoechea, Hector Casimiro; Gargallo, Raimundo; Skov, Thomas; Chemometrics: An important tool for monitoring interactions of vitamin B7 with bovine serum albumin with the aim of developing an efficient biosensing system for the analysis of protein; Elsevier; Talanta; 132; 1-2015; 354-365
0039-9140
url http://hdl.handle.net/11336/17015
identifier_str_mv Gholivand, Mohammad Bagher; Jalalvand, Ali R.; Goicoechea, Hector Casimiro; Gargallo, Raimundo; Skov, Thomas; Chemometrics: An important tool for monitoring interactions of vitamin B7 with bovine serum albumin with the aim of developing an efficient biosensing system for the analysis of protein; Elsevier; Talanta; 132; 1-2015; 354-365
0039-9140
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.talanta.2014.09.019
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0039914014007851
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
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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