Extending the hydrophobic mismatch concept to amphiphilic membranolytic peptides

A series of nine amphiphilic, pore-forming α-helical KIA peptides (KIAGKIA repeats) with lengths between 14 and 28 residues were studied by solidstate 15N NMR to determine their alignment in oriented lipid bilayers. In a 2:1 mixture of 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine (DMPC) with its...

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Detalles Bibliográficos
Autores: Grau Campistany, Ariadna, Strandberg, Erik, Wadhwani, Parvesh, Rabanal Anglada, Francesc, Ulrich, Anne S.
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2016
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/108766
Acceso en línea:https://hdl.handle.net/2445/108766
Access Level:acceso abierto
Palabra clave:Pèptids
Membranes (Biologia)
Bicapes lipídiques
Biofísica
Peptides
Membranes (Biology)
Lipid bilayers
Biophysics
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spelling Extending the hydrophobic mismatch concept to amphiphilic membranolytic peptidesGrau Campistany, AriadnaStrandberg, ErikWadhwani, ParveshRabanal Anglada, FrancescUlrich, Anne S.PèptidsMembranes (Biologia)Bicapes lipídiquesBiofísicaPeptidesMembranes (Biology)Lipid bilayersBiophysicsA series of nine amphiphilic, pore-forming α-helical KIA peptides (KIAGKIA repeats) with lengths between 14 and 28 residues were studied by solidstate 15N NMR to determine their alignment in oriented lipid bilayers. In a 2:1 mixture of 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine (DMPC) with its corresponding 1- myristoyl-2-hydroxy-sn-glycero-3-phosphocholine (lyso-MPC), which has a highly positive spontaneous curvature, the helix tilt angle was found to vary steadily with peptide length. The shortest peptide was aligned transmembrane and upright, while the longer ones successively became tilted away from the membrane normal. This behavior is in agreement with the hydrophobic matching concept, conceived so far only for hydrophobic helices. In 1,2-dioleoyl-sn-glycero-3-phosphatidylcholine, with a negative spontaneous curvature, all KIA peptides remained flat on the bilayer surface, while the cylindrical DMPC lipids permitted a slight tilt. Peptide insertion thus depends critically on the intrinsic lipid curvature, and helix orientation is then fine-tuned by membrane thickness. A refined toroidal pore model is proposed.American Chemical Society2016info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionapplication/pdfhttps://hdl.handle.net/2445/108766Articles publicats en revistes (Química Inorgànica i Orgànica)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésVersió postprint del document publicat a: https://doi.org/10.1021/acs.jpclett.6b00136Journal of Physical Chemistry Letters, 2016, vol. 7, num. 7, p. 1116-1120https://doi.org/10.1021/acs.jpclett.6b00136(c) American Chemical Society , 2016info:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/1087662026-05-27T06:46:51Z
dc.title.none.fl_str_mv Extending the hydrophobic mismatch concept to amphiphilic membranolytic peptides
title Extending the hydrophobic mismatch concept to amphiphilic membranolytic peptides
spellingShingle Extending the hydrophobic mismatch concept to amphiphilic membranolytic peptides
Grau Campistany, Ariadna
Pèptids
Membranes (Biologia)
Bicapes lipídiques
Biofísica
Peptides
Membranes (Biology)
Lipid bilayers
Biophysics
title_short Extending the hydrophobic mismatch concept to amphiphilic membranolytic peptides
title_full Extending the hydrophobic mismatch concept to amphiphilic membranolytic peptides
title_fullStr Extending the hydrophobic mismatch concept to amphiphilic membranolytic peptides
title_full_unstemmed Extending the hydrophobic mismatch concept to amphiphilic membranolytic peptides
title_sort Extending the hydrophobic mismatch concept to amphiphilic membranolytic peptides
dc.creator.none.fl_str_mv Grau Campistany, Ariadna
Strandberg, Erik
Wadhwani, Parvesh
Rabanal Anglada, Francesc
Ulrich, Anne S.
author Grau Campistany, Ariadna
author_facet Grau Campistany, Ariadna
Strandberg, Erik
Wadhwani, Parvesh
Rabanal Anglada, Francesc
Ulrich, Anne S.
author_role author
author2 Strandberg, Erik
Wadhwani, Parvesh
Rabanal Anglada, Francesc
Ulrich, Anne S.
author2_role author
author
author
author
dc.subject.none.fl_str_mv Pèptids
Membranes (Biologia)
Bicapes lipídiques
Biofísica
Peptides
Membranes (Biology)
Lipid bilayers
Biophysics
topic Pèptids
Membranes (Biologia)
Bicapes lipídiques
Biofísica
Peptides
Membranes (Biology)
Lipid bilayers
Biophysics
description A series of nine amphiphilic, pore-forming α-helical KIA peptides (KIAGKIA repeats) with lengths between 14 and 28 residues were studied by solidstate 15N NMR to determine their alignment in oriented lipid bilayers. In a 2:1 mixture of 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine (DMPC) with its corresponding 1- myristoyl-2-hydroxy-sn-glycero-3-phosphocholine (lyso-MPC), which has a highly positive spontaneous curvature, the helix tilt angle was found to vary steadily with peptide length. The shortest peptide was aligned transmembrane and upright, while the longer ones successively became tilted away from the membrane normal. This behavior is in agreement with the hydrophobic matching concept, conceived so far only for hydrophobic helices. In 1,2-dioleoyl-sn-glycero-3-phosphatidylcholine, with a negative spontaneous curvature, all KIA peptides remained flat on the bilayer surface, while the cylindrical DMPC lipids permitted a slight tilt. Peptide insertion thus depends critically on the intrinsic lipid curvature, and helix orientation is then fine-tuned by membrane thickness. A refined toroidal pore model is proposed.
publishDate 2016
dc.date.none.fl_str_mv 2016
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/108766
url https://hdl.handle.net/2445/108766
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Versió postprint del document publicat a: https://doi.org/10.1021/acs.jpclett.6b00136
Journal of Physical Chemistry Letters, 2016, vol. 7, num. 7, p. 1116-1120
https://doi.org/10.1021/acs.jpclett.6b00136
dc.rights.none.fl_str_mv (c) American Chemical Society , 2016
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) American Chemical Society , 2016
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv Articles publicats en revistes (Química Inorgànica i Orgànica)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,301603

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