Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis

Autores
Fernandez, Ariel; Berry, Stephen R.
Año de publicación
2003
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
We noticed that disease-related amyloidogenic proteins and especially cellular prion proteins have the highest proportion of incompletely desolvated backbone H bonds among soluble proteins. Such bonds are vulnerable to water attack and thus represent structural weaknesses. We have measured the adsorption of proteins onto phospholipid bilayers and found a strong correlation between the extent of underwrapping of backbone H bonds in the native structure of a protein and its extent of deposition on the bilayer: the less the H bond wrapping, the higher the propensity for protein-bilayer binding. These observations support the proposition that soluble proteins with amyloidogenic propensity and membrane proteins share a pervasive building motif: the underwrapped H bonds. Whereas in membrane proteins, this motif does not signal a structural vulnerability, in soluble proteins, it is responsible for their reactivity.
Fil: Fernandez, Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; Argentina. University of Chicago; Estados Unidos
Fil: Berry, Stephen R.. University of Chicago; Estados Unidos
Materia
Amyloid
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:11336/78919
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesisFernandez, ArielBerry, Stephen R.Amyloidhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1We noticed that disease-related amyloidogenic proteins and especially cellular prion proteins have the highest proportion of incompletely desolvated backbone H bonds among soluble proteins. Such bonds are vulnerable to water attack and thus represent structural weaknesses. We have measured the adsorption of proteins onto phospholipid bilayers and found a strong correlation between the extent of underwrapping of backbone H bonds in the native structure of a protein and its extent of deposition on the bilayer: the less the H bond wrapping, the higher the propensity for protein-bilayer binding. These observations support the proposition that soluble proteins with amyloidogenic propensity and membrane proteins share a pervasive building motif: the underwrapped H bonds. Whereas in membrane proteins, this motif does not signal a structural vulnerability, in soluble proteins, it is responsible for their reactivity.Fil: Fernandez, Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; Argentina. University of Chicago; Estados UnidosFil: Berry, Stephen R.. University of Chicago; Estados UnidosNational Academy of Sciences2003-03-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/78919Fernandez, Ariel; Berry, Stephen R.; Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 100; 5; 4-3-2003; 2391-23960027-8424ElectronicCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.pnas.org/content/100/5/2391info:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.0335642100info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-11-12T09:54:22Zoai:ri.conicet.gov.ar:11336/78919instacron: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:34982025-11-12 09:54:22.447CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis
title Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis
spellingShingle Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis
Fernandez, Ariel
Amyloid
title_short Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis
title_full Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis
title_fullStr Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis
title_full_unstemmed Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis
title_sort Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis
dc.creator.none.fl_str_mv Fernandez, Ariel
Berry, Stephen R.
author Fernandez, Ariel
author_facet Fernandez, Ariel
Berry, Stephen R.
author_role author
author2 Berry, Stephen R.
author2_role author
dc.subject.none.fl_str_mv Amyloid
topic Amyloid
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv We noticed that disease-related amyloidogenic proteins and especially cellular prion proteins have the highest proportion of incompletely desolvated backbone H bonds among soluble proteins. Such bonds are vulnerable to water attack and thus represent structural weaknesses. We have measured the adsorption of proteins onto phospholipid bilayers and found a strong correlation between the extent of underwrapping of backbone H bonds in the native structure of a protein and its extent of deposition on the bilayer: the less the H bond wrapping, the higher the propensity for protein-bilayer binding. These observations support the proposition that soluble proteins with amyloidogenic propensity and membrane proteins share a pervasive building motif: the underwrapped H bonds. Whereas in membrane proteins, this motif does not signal a structural vulnerability, in soluble proteins, it is responsible for their reactivity.
Fil: Fernandez, Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; Argentina. University of Chicago; Estados Unidos
Fil: Berry, Stephen R.. University of Chicago; Estados Unidos
description We noticed that disease-related amyloidogenic proteins and especially cellular prion proteins have the highest proportion of incompletely desolvated backbone H bonds among soluble proteins. Such bonds are vulnerable to water attack and thus represent structural weaknesses. We have measured the adsorption of proteins onto phospholipid bilayers and found a strong correlation between the extent of underwrapping of backbone H bonds in the native structure of a protein and its extent of deposition on the bilayer: the less the H bond wrapping, the higher the propensity for protein-bilayer binding. These observations support the proposition that soluble proteins with amyloidogenic propensity and membrane proteins share a pervasive building motif: the underwrapped H bonds. Whereas in membrane proteins, this motif does not signal a structural vulnerability, in soluble proteins, it is responsible for their reactivity.
publishDate 2003
dc.date.none.fl_str_mv 2003-03-04
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/11336/78919
Fernandez, Ariel; Berry, Stephen R.; Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 100; 5; 4-3-2003; 2391-2396
0027-8424
Electronic
CONICET Digital
CONICET
url http://hdl.handle.net/11336/78919
identifier_str_mv Fernandez, Ariel; Berry, Stephen R.; Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 100; 5; 4-3-2003; 2391-2396
0027-8424
Electronic
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.pnas.org/content/100/5/2391
info:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.0335642100
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 National Academy of Sciences
publisher.none.fl_str_mv National Academy of Sciences
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 12.976206

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