Topographic analysis by atomic force microscopy of proteoliposomes matrix vesicle mimetics harboring TNAP and AnxA5

Autores
Bolean, Maytê; Borin, Ivana A.; Simão, Ana M. S.; Bottini, Massimo; Bagatolli, Luis Alberto; Hoylaerts, Marc F.; Millán, José Luis; Ciancaglini, Pietro
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Atomic force microscopy (AFM) is one of the most commonly used scanning probe microscopy techniques for nanoscale imaging and characterization of lipid-based particles. However, obtaining images of such particles using AFM is still a challenge. The present study extends the capabilities of AFM to the characterization of proteoliposomes, a special class of liposomes composed of lipids and proteins, mimicking matrix vesicles (MVs) involved in the biomineralization process. To this end, proteoliposomes were synthesized, composed of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and 1,2-dipalmitoyl-sn-glycero-3-phospho-L-serine (DPPS), with inserted tissue-nonspecific alkaline phosphatase (TNAP) and/or annexin V (AnxA5), both characteristic proteins of osteoblast-derived MVs. We then aimed to study how TNAP and AnxA5 insertion affects the proteoliposomes’ membrane properties and, in turn, interactions with type II collagen, thus mimicking early MV activity during biomineralization. AFM images of these proteoliposomes, acquired in dynamic mode, revealed the presence of surface protrusions with distinct viscoelasticity, thus suggesting that the presence of the proteins induced local changes in membrane fluidity. Surface protrusions were measurable in TNAP-proteoliposomes but barely detectable in AnxA5-proteoliposomes. More complex surface structures were observed for proteoliposomes harboring both TNAP and AnxA5 concomitantly, resulting in a lower affinity for type II collagen fibers compared to proteoliposomes harboring AnxA5 alone. The present study achieved the topographic analysis of lipid vesicles by direct visualization of structural changes, resulting from protein incorporation, without the need for fluorescent probes.
Fil: Bolean, Maytê. Universidade de Sao Paulo; Brasil
Fil: Borin, Ivana A.. Universidade de Sao Paulo; Brasil
Fil: Simão, Ana M. S.. Universidade de Sao Paulo; Brasil
Fil: Bottini, Massimo. University of Rome Tor Vergata; Italia. Sanford Burnham Prebys Medical Discovery Institute; Estados Unidos
Fil: Bagatolli, Luis Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. University of Southern Denmark; Dinamarca
Fil: Hoylaerts, Marc F.. University of Leuven; Bélgica
Fil: Millán, José Luis. Sanford Burnham Prebys Medical Discovery Institute; Estados Unidos
Fil: Ciancaglini, Pietro. Universidade de Sao Paulo; Brasil
Materia
Annexin V
Atomic Force Microscopy
Collagen
Matrix Vesicles
Proteoliposomes
Tissue-Nonspecific Alkaline Phosphatase
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:11336/63998
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/63998
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Topographic analysis by atomic force microscopy of proteoliposomes matrix vesicle mimetics harboring TNAP and AnxA5Bolean, MaytêBorin, Ivana A.Simão, Ana M. S.Bottini, MassimoBagatolli, Luis AlbertoHoylaerts, Marc F.Millán, José LuisCiancaglini, PietroAnnexin VAtomic Force MicroscopyCollagenMatrix VesiclesProteoliposomesTissue-Nonspecific Alkaline Phosphatasehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Atomic force microscopy (AFM) is one of the most commonly used scanning probe microscopy techniques for nanoscale imaging and characterization of lipid-based particles. However, obtaining images of such particles using AFM is still a challenge. The present study extends the capabilities of AFM to the characterization of proteoliposomes, a special class of liposomes composed of lipids and proteins, mimicking matrix vesicles (MVs) involved in the biomineralization process. To this end, proteoliposomes were synthesized, composed of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and 1,2-dipalmitoyl-sn-glycero-3-phospho-L-serine (DPPS), with inserted tissue-nonspecific alkaline phosphatase (TNAP) and/or annexin V (AnxA5), both characteristic proteins of osteoblast-derived MVs. We then aimed to study how TNAP and AnxA5 insertion affects the proteoliposomes’ membrane properties and, in turn, interactions with type II collagen, thus mimicking early MV activity during biomineralization. AFM images of these proteoliposomes, acquired in dynamic mode, revealed the presence of surface protrusions with distinct viscoelasticity, thus suggesting that the presence of the proteins induced local changes in membrane fluidity. Surface protrusions were measurable in TNAP-proteoliposomes but barely detectable in AnxA5-proteoliposomes. More complex surface structures were observed for proteoliposomes harboring both TNAP and AnxA5 concomitantly, resulting in a lower affinity for type II collagen fibers compared to proteoliposomes harboring AnxA5 alone. The present study achieved the topographic analysis of lipid vesicles by direct visualization of structural changes, resulting from protein incorporation, without the need for fluorescent probes.Fil: Bolean, Maytê. Universidade de Sao Paulo; BrasilFil: Borin, Ivana A.. Universidade de Sao Paulo; BrasilFil: Simão, Ana M. S.. Universidade de Sao Paulo; BrasilFil: Bottini, Massimo. University of Rome Tor Vergata; Italia. Sanford Burnham Prebys Medical Discovery Institute; Estados UnidosFil: Bagatolli, Luis Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. University of Southern Denmark; DinamarcaFil: Hoylaerts, Marc F.. University of Leuven; BélgicaFil: Millán, José Luis. Sanford Burnham Prebys Medical Discovery Institute; Estados UnidosFil: Ciancaglini, Pietro. Universidade de Sao Paulo; BrasilElsevier Science2017-10-23info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/63998Bolean, Maytê; Borin, Ivana A.; Simão, Ana M. S.; Bottini, Massimo; Bagatolli, Luis Alberto; et al.; Topographic analysis by atomic force microscopy of proteoliposomes matrix vesicle mimetics harboring TNAP and AnxA5; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1859; 10; 23-10-2017; 1911-19200005-2736CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2017.05.010info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0005273617301633info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:43:54Zoai:ri.conicet.gov.ar:11336/63998instacron: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 09:43:54.517CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Topographic analysis by atomic force microscopy of proteoliposomes matrix vesicle mimetics harboring TNAP and AnxA5
title Topographic analysis by atomic force microscopy of proteoliposomes matrix vesicle mimetics harboring TNAP and AnxA5
spellingShingle Topographic analysis by atomic force microscopy of proteoliposomes matrix vesicle mimetics harboring TNAP and AnxA5
Bolean, Maytê
Annexin V
Atomic Force Microscopy
Collagen
Matrix Vesicles
Proteoliposomes
Tissue-Nonspecific Alkaline Phosphatase
title_short Topographic analysis by atomic force microscopy of proteoliposomes matrix vesicle mimetics harboring TNAP and AnxA5
title_full Topographic analysis by atomic force microscopy of proteoliposomes matrix vesicle mimetics harboring TNAP and AnxA5
title_fullStr Topographic analysis by atomic force microscopy of proteoliposomes matrix vesicle mimetics harboring TNAP and AnxA5
title_full_unstemmed Topographic analysis by atomic force microscopy of proteoliposomes matrix vesicle mimetics harboring TNAP and AnxA5
title_sort Topographic analysis by atomic force microscopy of proteoliposomes matrix vesicle mimetics harboring TNAP and AnxA5
dc.creator.none.fl_str_mv Bolean, Maytê
Borin, Ivana A.
Simão, Ana M. S.
Bottini, Massimo
Bagatolli, Luis Alberto
Hoylaerts, Marc F.
Millán, José Luis
Ciancaglini, Pietro
author Bolean, Maytê
author_facet Bolean, Maytê
Borin, Ivana A.
Simão, Ana M. S.
Bottini, Massimo
Bagatolli, Luis Alberto
Hoylaerts, Marc F.
Millán, José Luis
Ciancaglini, Pietro
author_role author
author2 Borin, Ivana A.
Simão, Ana M. S.
Bottini, Massimo
Bagatolli, Luis Alberto
Hoylaerts, Marc F.
Millán, José Luis
Ciancaglini, Pietro
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Annexin V
Atomic Force Microscopy
Collagen
Matrix Vesicles
Proteoliposomes
Tissue-Nonspecific Alkaline Phosphatase
topic Annexin V
Atomic Force Microscopy
Collagen
Matrix Vesicles
Proteoliposomes
Tissue-Nonspecific Alkaline Phosphatase
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Atomic force microscopy (AFM) is one of the most commonly used scanning probe microscopy techniques for nanoscale imaging and characterization of lipid-based particles. However, obtaining images of such particles using AFM is still a challenge. The present study extends the capabilities of AFM to the characterization of proteoliposomes, a special class of liposomes composed of lipids and proteins, mimicking matrix vesicles (MVs) involved in the biomineralization process. To this end, proteoliposomes were synthesized, composed of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and 1,2-dipalmitoyl-sn-glycero-3-phospho-L-serine (DPPS), with inserted tissue-nonspecific alkaline phosphatase (TNAP) and/or annexin V (AnxA5), both characteristic proteins of osteoblast-derived MVs. We then aimed to study how TNAP and AnxA5 insertion affects the proteoliposomes’ membrane properties and, in turn, interactions with type II collagen, thus mimicking early MV activity during biomineralization. AFM images of these proteoliposomes, acquired in dynamic mode, revealed the presence of surface protrusions with distinct viscoelasticity, thus suggesting that the presence of the proteins induced local changes in membrane fluidity. Surface protrusions were measurable in TNAP-proteoliposomes but barely detectable in AnxA5-proteoliposomes. More complex surface structures were observed for proteoliposomes harboring both TNAP and AnxA5 concomitantly, resulting in a lower affinity for type II collagen fibers compared to proteoliposomes harboring AnxA5 alone. The present study achieved the topographic analysis of lipid vesicles by direct visualization of structural changes, resulting from protein incorporation, without the need for fluorescent probes.
Fil: Bolean, Maytê. Universidade de Sao Paulo; Brasil
Fil: Borin, Ivana A.. Universidade de Sao Paulo; Brasil
Fil: Simão, Ana M. S.. Universidade de Sao Paulo; Brasil
Fil: Bottini, Massimo. University of Rome Tor Vergata; Italia. Sanford Burnham Prebys Medical Discovery Institute; Estados Unidos
Fil: Bagatolli, Luis Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. University of Southern Denmark; Dinamarca
Fil: Hoylaerts, Marc F.. University of Leuven; Bélgica
Fil: Millán, José Luis. Sanford Burnham Prebys Medical Discovery Institute; Estados Unidos
Fil: Ciancaglini, Pietro. Universidade de Sao Paulo; Brasil
description Atomic force microscopy (AFM) is one of the most commonly used scanning probe microscopy techniques for nanoscale imaging and characterization of lipid-based particles. However, obtaining images of such particles using AFM is still a challenge. The present study extends the capabilities of AFM to the characterization of proteoliposomes, a special class of liposomes composed of lipids and proteins, mimicking matrix vesicles (MVs) involved in the biomineralization process. To this end, proteoliposomes were synthesized, composed of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and 1,2-dipalmitoyl-sn-glycero-3-phospho-L-serine (DPPS), with inserted tissue-nonspecific alkaline phosphatase (TNAP) and/or annexin V (AnxA5), both characteristic proteins of osteoblast-derived MVs. We then aimed to study how TNAP and AnxA5 insertion affects the proteoliposomes’ membrane properties and, in turn, interactions with type II collagen, thus mimicking early MV activity during biomineralization. AFM images of these proteoliposomes, acquired in dynamic mode, revealed the presence of surface protrusions with distinct viscoelasticity, thus suggesting that the presence of the proteins induced local changes in membrane fluidity. Surface protrusions were measurable in TNAP-proteoliposomes but barely detectable in AnxA5-proteoliposomes. More complex surface structures were observed for proteoliposomes harboring both TNAP and AnxA5 concomitantly, resulting in a lower affinity for type II collagen fibers compared to proteoliposomes harboring AnxA5 alone. The present study achieved the topographic analysis of lipid vesicles by direct visualization of structural changes, resulting from protein incorporation, without the need for fluorescent probes.
publishDate 2017
dc.date.none.fl_str_mv 2017-10-23
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/11336/63998
Bolean, Maytê; Borin, Ivana A.; Simão, Ana M. S.; Bottini, Massimo; Bagatolli, Luis Alberto; et al.; Topographic analysis by atomic force microscopy of proteoliposomes matrix vesicle mimetics harboring TNAP and AnxA5; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1859; 10; 23-10-2017; 1911-1920
0005-2736
CONICET Digital
CONICET
url http://hdl.handle.net/11336/63998
identifier_str_mv Bolean, Maytê; Borin, Ivana A.; Simão, Ana M. S.; Bottini, Massimo; Bagatolli, Luis Alberto; et al.; Topographic analysis by atomic force microscopy of proteoliposomes matrix vesicle mimetics harboring TNAP and AnxA5; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1859; 10; 23-10-2017; 1911-1920
0005-2736
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2017.05.010
info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0005273617301633
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 13.070432

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