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dc.contributor.author
Bortolus, Marco
dc.contributor.author
Dalzini, Annalisa
dc.contributor.author
Maniero, Anna Lisa
dc.contributor.author
Panighel, Giacomo
dc.contributor.author
Siano, Alvaro Sebastían
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dc.contributor.author
Toniolo, Claudio
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De Zotti, Marta
dc.contributor.author
Formaggio, Fernando
dc.date.available
2018-12-07T20:27:39Z
dc.date.issued
2017-01
dc.identifier.citation
Bortolus, Marco; Dalzini, Annalisa; Maniero, Anna Lisa; Panighel, Giacomo; Siano, Alvaro Sebastían; et al.; Insights into peptide-membrane interactions of newly synthesized, nitroxide-containing analogs of the peptaibiotic trichogin GA IV using EPR; John Wiley & Sons Inc; Biopolymers; 108; 1; 1-2017; 1-13
dc.identifier.issn
0006-3525
dc.identifier.uri
http://hdl.handle.net/11336/66107
dc.description.abstract
Trichogin GA IV is a short-length (10-amino acid long), mostly hydrophobic, peptaibiotic with an N-terminal fatty acyl chain and a C-terminal 1,2-amino alcohol. A cardinal role of the terminal moieties in the cytotoxic activity of trichogin has been recently found. Previously, peptide orientation and dynamics of trichogin analogs in the membrane were studied using methyl ester derivatives. Therefore, in the present work we synthesized several trichogin analogs with naturally occurring terminal groups to verify whether these moieties have any effect on peptide-membrane interaction. These trichogin analogs, both neutral and carrying a positively charged Lys residue, bear the nitroxide-containing α-amino acid TOAC to study them using EPR spectroscopy. Vesicles were used to investigate orientation and penetration depth of the peptide at room temperature. Bicelles were employed to evaluate the order, dynamics, and orientation of the peptide at a near physiological temperature. In addition, the position of the N-terminal 1-octanoyl chain in the membrane was studied by labeling it with a nitroxide. The secondary structure of the peptides in vesicles was studied by CD spectroscopy showing that they adopt a mostly α-helical structure. In vesicles, the analogs insert below the lipid headgroups with the helix axis oriented parallel to the membrane surface at a peptide-to-lipid (P:L) ratio of 1:100. The presence of the single, positively charged Lys residue does not alter the orientation adopted by the peptides. In bicelles at P:L ratios 1:100 and 1:60, the peptide adopts a transmembrane orientation characterized by a very low orientational order, whereas at a 1:15 P:L ratio it severely disrupts the membrane. Our data shows that overall orientation and insertion in model membranes of the native trichogin GA IV are strictly comparable to those of its methyl ester analogs previously examined.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
John Wiley & Sons Inc
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Bicelles
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Circular Dichroism
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Electron Paramagnetic Resonance
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Membranes
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Trichogin
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Otras Ciencias Químicas
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dc.subject.classification
Ciencias Químicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Insights into peptide-membrane interactions of newly synthesized, nitroxide-containing analogs of the peptaibiotic trichogin GA IV using EPR
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-11-27T16:34:16Z
dc.journal.volume
108
dc.journal.number
1
dc.journal.pagination
1-13
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Nueva York
dc.description.fil
Fil: Bortolus, Marco. Università di Padova; Italia
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Fil: Dalzini, Annalisa. Università di Padova; Italia
dc.description.fil
Fil: Maniero, Anna Lisa. Università di Padova; Italia
dc.description.fil
Fil: Panighel, Giacomo. Università di Padova; Italia
dc.description.fil
Fil: Siano, Alvaro Sebastían. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Química Organica. Laboratorio de Peptidos Bioactivos; Argentina. Università di Padova; Italia
dc.description.fil
Fil: Toniolo, Claudio. Università di Padova; Italia. Institute of Biomolecular Chemistry; Italia
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Fil: De Zotti, Marta. Università di Padova; Italia
dc.description.fil
Fil: Formaggio, Fernando. Università di Padova; Italia. Institute of Biomolecular Chemistry; Italia
dc.journal.title
Biopolymers
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/bip.22913
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1002/bip.22913
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