Polyethyleneimine-protein interactions and implications on protein stability

Autores
Mazzaferro, Laura; Breccia, Javier Dario; Andersson, Maria M.; Hitzmann, Bernd; Hatti Kaul, Rajni
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Protein stability assessment of seven model proteins in the presence of low molecular weight polyethyleneimine (PEI, MW 2000Da) was performed. Thermodynamic stability, monitored by circular dichroism (CD) spectroscopy, showed that the polymer did not have a major effect on the melting temperature (T m ) of the basic proteins - muscle lactate dehydrogenase (LDH), ribonuclease A, lysozyme and cutinase, while for the acidic ones - human growth hormone, human serum albumin and heart lactate dehydrogenase - there was a shift in T m towards lower temperatures. The secondary structures of the basic proteins were essentially the same, with none or a slight increase in the CD spectra, in presence of the polymer. In the case of the acidic proteins, the CD spectra were diminished mostly due to phase separation. Assuming a homogeneous distribution of the net charge on the protein surface a quantitative inverse relationship was established between surface charge density of the acidic proteins and the PEI 2000 concentration required for maximum flocculation. Despite lowering the thermal stability of acidic proteins, PEI 2000 was seen to protect heart LDH at an increasing oxidative stress.
Fil: Mazzaferro, Laura. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Departamento de Química; Argentina
Fil: Breccia, Javier Dario. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Departamento de Química; Argentina
Fil: Andersson, Maria M.. Lund University; Suecia
Fil: Hitzmann, Bernd. Universität Hannover; Alemania
Fil: Hatti Kaul, Rajni. Lund University; Suecia
Materia
Oxidation
Polycation
Thermodynamic Stability
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:11336/81594
Acceder
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spelling Polyethyleneimine-protein interactions and implications on protein stabilityMazzaferro, LauraBreccia, Javier DarioAndersson, Maria M.Hitzmann, BerndHatti Kaul, RajniOxidationPolycationThermodynamic Stabilityhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Protein stability assessment of seven model proteins in the presence of low molecular weight polyethyleneimine (PEI, MW 2000Da) was performed. Thermodynamic stability, monitored by circular dichroism (CD) spectroscopy, showed that the polymer did not have a major effect on the melting temperature (T m ) of the basic proteins - muscle lactate dehydrogenase (LDH), ribonuclease A, lysozyme and cutinase, while for the acidic ones - human growth hormone, human serum albumin and heart lactate dehydrogenase - there was a shift in T m towards lower temperatures. The secondary structures of the basic proteins were essentially the same, with none or a slight increase in the CD spectra, in presence of the polymer. In the case of the acidic proteins, the CD spectra were diminished mostly due to phase separation. Assuming a homogeneous distribution of the net charge on the protein surface a quantitative inverse relationship was established between surface charge density of the acidic proteins and the PEI 2000 concentration required for maximum flocculation. Despite lowering the thermal stability of acidic proteins, PEI 2000 was seen to protect heart LDH at an increasing oxidative stress.Fil: Mazzaferro, Laura. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Departamento de Química; ArgentinaFil: Breccia, Javier Dario. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Departamento de Química; ArgentinaFil: Andersson, Maria M.. Lund University; SueciaFil: Hitzmann, Bernd. Universität Hannover; AlemaniaFil: Hatti Kaul, Rajni. Lund University; SueciaElsevier Science2010-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/81594Mazzaferro, Laura; Breccia, Javier Dario; Andersson, Maria M.; Hitzmann, Bernd; Hatti Kaul, Rajni; Polyethyleneimine-protein interactions and implications on protein stability; Elsevier Science; International Journal of Biological Macromolecules; 47; 1; 7-2010; 15-200141-8130CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141813010001212info:eu-repo/semantics/altIdentifier/doi/10.1016/j.ijbiomac.2010.04.003info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:10:59Zoai:ri.conicet.gov.ar:11336/81594instacron: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:34982025-10-15 15:10:59.836CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Polyethyleneimine-protein interactions and implications on protein stability
title Polyethyleneimine-protein interactions and implications on protein stability
spellingShingle Polyethyleneimine-protein interactions and implications on protein stability
Mazzaferro, Laura
Oxidation
Polycation
Thermodynamic Stability
title_short Polyethyleneimine-protein interactions and implications on protein stability
title_full Polyethyleneimine-protein interactions and implications on protein stability
title_fullStr Polyethyleneimine-protein interactions and implications on protein stability
title_full_unstemmed Polyethyleneimine-protein interactions and implications on protein stability
title_sort Polyethyleneimine-protein interactions and implications on protein stability
dc.creator.none.fl_str_mv Mazzaferro, Laura
Breccia, Javier Dario
Andersson, Maria M.
Hitzmann, Bernd
Hatti Kaul, Rajni
author Mazzaferro, Laura
author_facet Mazzaferro, Laura
Breccia, Javier Dario
Andersson, Maria M.
Hitzmann, Bernd
Hatti Kaul, Rajni
author_role author
author2 Breccia, Javier Dario
Andersson, Maria M.
Hitzmann, Bernd
Hatti Kaul, Rajni
author2_role author
author
author
author
dc.subject.none.fl_str_mv Oxidation
Polycation
Thermodynamic Stability
topic Oxidation
Polycation
Thermodynamic Stability
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Protein stability assessment of seven model proteins in the presence of low molecular weight polyethyleneimine (PEI, MW 2000Da) was performed. Thermodynamic stability, monitored by circular dichroism (CD) spectroscopy, showed that the polymer did not have a major effect on the melting temperature (T m ) of the basic proteins - muscle lactate dehydrogenase (LDH), ribonuclease A, lysozyme and cutinase, while for the acidic ones - human growth hormone, human serum albumin and heart lactate dehydrogenase - there was a shift in T m towards lower temperatures. The secondary structures of the basic proteins were essentially the same, with none or a slight increase in the CD spectra, in presence of the polymer. In the case of the acidic proteins, the CD spectra were diminished mostly due to phase separation. Assuming a homogeneous distribution of the net charge on the protein surface a quantitative inverse relationship was established between surface charge density of the acidic proteins and the PEI 2000 concentration required for maximum flocculation. Despite lowering the thermal stability of acidic proteins, PEI 2000 was seen to protect heart LDH at an increasing oxidative stress.
Fil: Mazzaferro, Laura. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Departamento de Química; Argentina
Fil: Breccia, Javier Dario. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Departamento de Química; Argentina
Fil: Andersson, Maria M.. Lund University; Suecia
Fil: Hitzmann, Bernd. Universität Hannover; Alemania
Fil: Hatti Kaul, Rajni. Lund University; Suecia
description Protein stability assessment of seven model proteins in the presence of low molecular weight polyethyleneimine (PEI, MW 2000Da) was performed. Thermodynamic stability, monitored by circular dichroism (CD) spectroscopy, showed that the polymer did not have a major effect on the melting temperature (T m ) of the basic proteins - muscle lactate dehydrogenase (LDH), ribonuclease A, lysozyme and cutinase, while for the acidic ones - human growth hormone, human serum albumin and heart lactate dehydrogenase - there was a shift in T m towards lower temperatures. The secondary structures of the basic proteins were essentially the same, with none or a slight increase in the CD spectra, in presence of the polymer. In the case of the acidic proteins, the CD spectra were diminished mostly due to phase separation. Assuming a homogeneous distribution of the net charge on the protein surface a quantitative inverse relationship was established between surface charge density of the acidic proteins and the PEI 2000 concentration required for maximum flocculation. Despite lowering the thermal stability of acidic proteins, PEI 2000 was seen to protect heart LDH at an increasing oxidative stress.
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/11336/81594
Mazzaferro, Laura; Breccia, Javier Dario; Andersson, Maria M.; Hitzmann, Bernd; Hatti Kaul, Rajni; Polyethyleneimine-protein interactions and implications on protein stability; Elsevier Science; International Journal of Biological Macromolecules; 47; 1; 7-2010; 15-20
0141-8130
CONICET Digital
CONICET
url http://hdl.handle.net/11336/81594
identifier_str_mv Mazzaferro, Laura; Breccia, Javier Dario; Andersson, Maria M.; Hitzmann, Bernd; Hatti Kaul, Rajni; Polyethyleneimine-protein interactions and implications on protein stability; Elsevier Science; International Journal of Biological Macromolecules; 47; 1; 7-2010; 15-20
0141-8130
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141813010001212
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.ijbiomac.2010.04.003
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 Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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 13.22299

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