Micelle-Triggered b-Hairpin to a-Helix Transition in a 14-Residue Peptide from aBinding Choline- Repeat of the Pneumococcal Autolysin LytA

Choline-binding modules (CBMs) have a bb-solenoid structure composed of choline-binding repeats (CBR), which consist of a b-hairpin followed by a short linker. To find minimal peptides that are able to maintain the CBR native structure and to evaluate their remaining cholinebinding ability, we have...

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Autores: Zamora-Carreras, Héctor, Maestro, Beatriz, Strandberg, Erik, Ulrich, Anne S., Sanz, Jesús M., Jiménez, M. Ángeles
Tipo de recurso: artículo
Fecha de publicación:2015
País:España
Institución:Universidad Miguel Hernández de Elche
Repositorio:REDIUMH. Depósito Digital de la UMH
OAI Identifier:oai:dspace.umh.es:11000/30956
Acceso en línea:https://hdl.handle.net/11000/30956
Access Level:acceso abierto
Palabra clave:micelles
protein folding
protein structures
structural biology
structural elucidation
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spelling Micelle-Triggered b-Hairpin to a-Helix Transition in a 14-Residue Peptide from aBinding Choline- Repeat of the Pneumococcal Autolysin LytAZamora-Carreras, HéctorMaestro, BeatrizStrandberg, ErikUlrich, Anne S.Sanz, Jesús M.Jiménez, M. Ángelesmicellesprotein foldingprotein structuresstructural biologystructural elucidationCholine-binding modules (CBMs) have a bb-solenoid structure composed of choline-binding repeats (CBR), which consist of a b-hairpin followed by a short linker. To find minimal peptides that are able to maintain the CBR native structure and to evaluate their remaining cholinebinding ability, we have analysed the third b-hairpin of the CBM from the pneumococcal LytA autolysin. Circular dichroism and NMR data reveal that this peptide forms a highly stable native-like b-hairpin both in aqueous solution and in the presence of trifluoroethanol, but, strikingly, the peptide structure is a stable amphipathic a-helix in both zwitterionic (dodecylphosphocholine) and anionic (sodium dodecylsulfate) detergent micelles, as well as in small unilamellar vesicles. This b-hairpin to a-helix conversion is reversible. Given that the b-hairpin and a-helix differ greatly in the distribution of hydrophobic and hydrophilic side chains, we propose that the amphipathicity is a requirement for a peptide structure to interact and to be stable in micelles or lipid vesicles. To our knowledge, this “chameleonic” behaviour is the only described case of a micelle-induced structural transition between two ordered peptide structures.Willey on line LibraryInstitutos de la UMH::Instituto de Bioingeniería202420242015info:eu-repo/semantics/articleapplication/pdf30application/pdfhttps://hdl.handle.net/11000/30956reponame:REDIUMH. Depósito Digital de la UMHinstname:Universidad Miguel Hernández de ElcheIngléshttps://doi.org/10.1002/chem.201500447info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/4.0/oai:dspace.umh.es:11000/309562026-05-27T13:36:21Z
dc.title.none.fl_str_mv Micelle-Triggered b-Hairpin to a-Helix Transition in a 14-Residue Peptide from aBinding Choline- Repeat of the Pneumococcal Autolysin LytA
title Micelle-Triggered b-Hairpin to a-Helix Transition in a 14-Residue Peptide from aBinding Choline- Repeat of the Pneumococcal Autolysin LytA
spellingShingle Micelle-Triggered b-Hairpin to a-Helix Transition in a 14-Residue Peptide from aBinding Choline- Repeat of the Pneumococcal Autolysin LytA
Zamora-Carreras, Héctor
micelles
protein folding
protein structures
structural biology
structural elucidation
title_short Micelle-Triggered b-Hairpin to a-Helix Transition in a 14-Residue Peptide from aBinding Choline- Repeat of the Pneumococcal Autolysin LytA
title_full Micelle-Triggered b-Hairpin to a-Helix Transition in a 14-Residue Peptide from aBinding Choline- Repeat of the Pneumococcal Autolysin LytA
title_fullStr Micelle-Triggered b-Hairpin to a-Helix Transition in a 14-Residue Peptide from aBinding Choline- Repeat of the Pneumococcal Autolysin LytA
title_full_unstemmed Micelle-Triggered b-Hairpin to a-Helix Transition in a 14-Residue Peptide from aBinding Choline- Repeat of the Pneumococcal Autolysin LytA
title_sort Micelle-Triggered b-Hairpin to a-Helix Transition in a 14-Residue Peptide from aBinding Choline- Repeat of the Pneumococcal Autolysin LytA
dc.creator.none.fl_str_mv Zamora-Carreras, Héctor
Maestro, Beatriz
Strandberg, Erik
Ulrich, Anne S.
Sanz, Jesús M.
Jiménez, M. Ángeles
author Zamora-Carreras, Héctor
author_facet Zamora-Carreras, Héctor
Maestro, Beatriz
Strandberg, Erik
Ulrich, Anne S.
Sanz, Jesús M.
Jiménez, M. Ángeles
author_role author
author2 Maestro, Beatriz
Strandberg, Erik
Ulrich, Anne S.
Sanz, Jesús M.
Jiménez, M. Ángeles
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Institutos de la UMH::Instituto de Bioingeniería
dc.subject.none.fl_str_mv micelles
protein folding
protein structures
structural biology
structural elucidation
topic micelles
protein folding
protein structures
structural biology
structural elucidation
description Choline-binding modules (CBMs) have a bb-solenoid structure composed of choline-binding repeats (CBR), which consist of a b-hairpin followed by a short linker. To find minimal peptides that are able to maintain the CBR native structure and to evaluate their remaining cholinebinding ability, we have analysed the third b-hairpin of the CBM from the pneumococcal LytA autolysin. Circular dichroism and NMR data reveal that this peptide forms a highly stable native-like b-hairpin both in aqueous solution and in the presence of trifluoroethanol, but, strikingly, the peptide structure is a stable amphipathic a-helix in both zwitterionic (dodecylphosphocholine) and anionic (sodium dodecylsulfate) detergent micelles, as well as in small unilamellar vesicles. This b-hairpin to a-helix conversion is reversible. Given that the b-hairpin and a-helix differ greatly in the distribution of hydrophobic and hydrophilic side chains, we propose that the amphipathicity is a requirement for a peptide structure to interact and to be stable in micelles or lipid vesicles. To our knowledge, this “chameleonic” behaviour is the only described case of a micelle-induced structural transition between two ordered peptide structures.
publishDate 2015
dc.date.none.fl_str_mv 2015
2024
2024
dc.type.none.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/11000/30956
url https://hdl.handle.net/11000/30956
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv https://doi.org/10.1002/chem.201500447
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.format.none.fl_str_mv application/pdf
30
application/pdf
dc.publisher.none.fl_str_mv Willey on line Library
publisher.none.fl_str_mv Willey on line Library
dc.source.none.fl_str_mv reponame:REDIUMH. Depósito Digital de la UMH
instname:Universidad Miguel Hernández de Elche
instname_str Universidad Miguel Hernández de Elche
reponame_str REDIUMH. Depósito Digital de la UMH
collection REDIUMH. Depósito Digital de la UMH
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,300719

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