Binary Exo-Chiralities in the Peptide α-Helix Studied by Circular Dichroism

Chirality is a property present across all scales, from the atomic to the macroscopic world, that mediates crucial processes such as drug recognition, plant growth or transcription of genetic information. Living beings are homochiral, since nature has evolved into a single handedness that can be tra...

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Detalles Bibliográficos
Autor: Gómez Ojea, Rebeca
Tipo de recurso: tesis doctoral
Fecha de publicación:2025
País:España
Institución:Universidad de Santiago de Compostela (USC)
Repositorio:Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
Idioma:inglés
OAI Identifier:oai:dnet:minerva_____::4f3fbf9069e4edb1df82118d48b43d58
Acceso en línea:https://hdl.handle.net/10347/42526
Access Level:acceso abierto
Palabra clave:peptides
chirality
exohelix
circular dichroism
230224 Péptidos
230616 Esteroquímica y análisis conformacional
230409 Modificación de macromoléculas
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spelling Binary Exo-Chiralities in the Peptide α-Helix Studied by Circular DichroismGómez Ojea, Rebecapeptideschiralityexohelixcircular dichroism230224 Péptidos230616 Esteroquímica y análisis conformacional230409 Modificación de macromoléculasChirality is a property present across all scales, from the atomic to the macroscopic world, that mediates crucial processes such as drug recognition, plant growth or transcription of genetic information. Living beings are homochiral, since nature has evolved into a single handedness that can be transmitted from the monomers to macromolecules such as alpha helical peptides, mostly present in nature folded into right handed helices. These supramolecular chiral structures expose functional groups from the monomer sidechains towards the exterior of the helix, creating another layer of information on its surface. Such information can be topologically distributed and is crucial for peptide functionality and assembly into higher order structures. Chiral complex topologies, like binary exohelical ones, represent a superior level of biomacromolecular chirality and constitute the main focus of this thesis. Small alpha helical peptides emerge as the perfect templates for studying these exochiralities and their combination. Solid phase peptide synthesis inherent sequence control allows the creation of tailored unique exohelices based on different repetition patterns. Side chain functionalization of amino acids in these repeated positions with chromophores allows structural elucidation of such exohelices by circular dichroism.Montenegro García, JavierBergueiro Álvarez, JuliánUniversidade de Santiago de Compostela. Escola de Doutoramento Internacional (EDIUS)Granja Guillán, Juan Ramón20252025-01-0120252025-01-01doctoral thesishttp://purl.org/coar/resource_type/c_db06info:eu-repo/semantics/doctoralThesisapplication/pdfhttps://hdl.handle.net/10347/42526reponame:Minerva. Repositorio Institucional de la Universidad de Santiago de Compostelainstname:Universidad de Santiago de Compostela (USC)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:dnet:minerva_____::4f3fbf9069e4edb1df82118d48b43d582026-06-15T12:47:27Z
dc.title.none.fl_str_mv Binary Exo-Chiralities in the Peptide α-Helix Studied by Circular Dichroism
title Binary Exo-Chiralities in the Peptide α-Helix Studied by Circular Dichroism
spellingShingle Binary Exo-Chiralities in the Peptide α-Helix Studied by Circular Dichroism
Gómez Ojea, Rebeca
peptides
chirality
exohelix
circular dichroism
230224 Péptidos
230616 Esteroquímica y análisis conformacional
230409 Modificación de macromoléculas
title_short Binary Exo-Chiralities in the Peptide α-Helix Studied by Circular Dichroism
title_full Binary Exo-Chiralities in the Peptide α-Helix Studied by Circular Dichroism
title_fullStr Binary Exo-Chiralities in the Peptide α-Helix Studied by Circular Dichroism
title_full_unstemmed Binary Exo-Chiralities in the Peptide α-Helix Studied by Circular Dichroism
title_sort Binary Exo-Chiralities in the Peptide α-Helix Studied by Circular Dichroism
dc.creator.none.fl_str_mv Gómez Ojea, Rebeca
author Gómez Ojea, Rebeca
author_facet Gómez Ojea, Rebeca
author_role author
dc.contributor.none.fl_str_mv Montenegro García, Javier
Bergueiro Álvarez, Julián
Universidade de Santiago de Compostela. Escola de Doutoramento Internacional (EDIUS)
Granja Guillán, Juan Ramón
dc.subject.none.fl_str_mv peptides
chirality
exohelix
circular dichroism
230224 Péptidos
230616 Esteroquímica y análisis conformacional
230409 Modificación de macromoléculas
topic peptides
chirality
exohelix
circular dichroism
230224 Péptidos
230616 Esteroquímica y análisis conformacional
230409 Modificación de macromoléculas
description Chirality is a property present across all scales, from the atomic to the macroscopic world, that mediates crucial processes such as drug recognition, plant growth or transcription of genetic information. Living beings are homochiral, since nature has evolved into a single handedness that can be transmitted from the monomers to macromolecules such as alpha helical peptides, mostly present in nature folded into right handed helices. These supramolecular chiral structures expose functional groups from the monomer sidechains towards the exterior of the helix, creating another layer of information on its surface. Such information can be topologically distributed and is crucial for peptide functionality and assembly into higher order structures. Chiral complex topologies, like binary exohelical ones, represent a superior level of biomacromolecular chirality and constitute the main focus of this thesis. Small alpha helical peptides emerge as the perfect templates for studying these exochiralities and their combination. Solid phase peptide synthesis inherent sequence control allows the creation of tailored unique exohelices based on different repetition patterns. Side chain functionalization of amino acids in these repeated positions with chromophores allows structural elucidation of such exohelices by circular dichroism.
publishDate 2025
dc.date.none.fl_str_mv 2025
2025-01-01
2025
2025-01-01
dc.type.none.fl_str_mv doctoral thesis
http://purl.org/coar/resource_type/c_db06
dc.type.openaire.fl_str_mv info:eu-repo/semantics/doctoralThesis
format doctoralThesis
dc.identifier.none.fl_str_mv https://hdl.handle.net/10347/42526
url https://hdl.handle.net/10347/42526
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
instname:Universidad de Santiago de Compostela (USC)
instname_str Universidad de Santiago de Compostela (USC)
reponame_str Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
collection Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
repository.name.fl_str_mv
repository.mail.fl_str_mv
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