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dc.contributor.author
Salnikov, Evgeniy S.
dc.contributor.author
De Zotti, Marta
dc.contributor.author
Bobone, Sara
dc.contributor.author
Mazzuca, Claudia
dc.contributor.author
Raya, Jesus
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Siano, Alvaro Sebastían
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Peggion, Cristina
dc.contributor.author
Toniolo, Claudio
dc.contributor.author
Stella, Lorenzo
dc.contributor.author
Bechinger, Burkhard
dc.date.available
2022-02-02T13:04:29Z
dc.date.issued
2019-05
dc.identifier.citation
Salnikov, Evgeniy S.; De Zotti, Marta; Bobone, Sara; Mazzuca, Claudia; Raya, Jesus; et al.; Trichogin GA IV Alignment and Oligomerization in Phospholipid Bilayers; Wiley VCH Verlag; Chembiochem; 20; 16; 5-2019; 2141-2150
dc.identifier.issn
1439-4227
dc.identifier.uri
http://hdl.handle.net/11336/151164
dc.description.abstract
Trichogin GA IV is a short peptaibol with antimicrobial activity. This uncharged, but amphipathic, sequence is aligned at the membrane interface and undergoes a transition to an aggregated state that inserts more deeply into the membrane, an assembly that predominates at a peptide-to-lipid ratio (P/L) of 1:20. In this work, the natural trichogin sequence was prepared and reconstituted into oriented lipid bilayers. The 15N NMR chemical shift is indicative of a well-defined alignment of the peptide parallel to the membrane surface at P/Ls of 1:120 and 1:20. When the P/L is increased to 1:8, an additional peptide topology is observed that is indicative of a heterogeneous orientation, with helix alignments ranging from around the magic angle to perfectly in-plane. The topological preference of the trichogin helix for an orientation parallel to the membrane surface was confirmed by attenuated total reflection FTIR spectroscopy. Furthermore, 19F CODEX experiments were performed on a trichogin sequence with 19F-Phe at position 10. The CODEX decay is in agreement with a tetrameric complex, in which the 19F sites are about 9–9.5 Å apart. Thus, a model emerges in which the monomeric peptide aligns along the membrane surface. When the peptide concentration increases, first dimeric and then tetrameric assemblies form, made up from helices oriented predominantly parallel to the membrane surface. The formation of these aggregates correlates with the release of vesicle contents including relatively large molecules.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley VCH Verlag
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
ANTIMICROBIAL PEPTIDES
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ATR FTIR SPECTROSCOPY
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LIPID BILAYERS
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MEMBRANE PERMEABILIZATION
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SOLID-STATE NMR SPECTROSCOPY
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Química Orgánica
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Ciencias Químicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Trichogin GA IV Alignment and Oligomerization in Phospholipid Bilayers
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-11-18T21:19:44Z
dc.journal.volume
20
dc.journal.number
16
dc.journal.pagination
2141-2150
dc.journal.pais
Alemania
dc.journal.ciudad
Weinheim
dc.description.fil
Fil: Salnikov, Evgeniy S.. Université de Strasbourg; Francia
dc.description.fil
Fil: De Zotti, Marta. Università di Padova; Italia
dc.description.fil
Fil: Bobone, Sara. Universita Tor Vergata; Italia
dc.description.fil
Fil: Mazzuca, Claudia. Universita Tor Vergata; Italia
dc.description.fil
Fil: Raya, Jesus. Université de Strasbourg; Francia
dc.description.fil
Fil: Siano, Alvaro Sebastían. Universidad Nacional del Litoral; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina
dc.description.fil
Fil: Peggion, Cristina. Università di Padova; Italia
dc.description.fil
Fil: Toniolo, Claudio. Università di Padova; Italia
dc.description.fil
Fil: Stella, Lorenzo. Universita Tor Vergata; Italia
dc.description.fil
Fil: Bechinger, Burkhard. Université de Strasbourg; Francia
dc.journal.title
Chembiochem
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1002/cbic.201900263
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