Study of biomolecular self-assembly and host-guest association using spectroscopic and microscopic techniques

dc.contributor.advisorRodríguez-Prieto, Flor
dc.contributor.advisorNovo, Mercedes
dc.contributor.affiliationUniversidade de Santiago de Compostela. Escola de Doutoramento Internacional (EDIUS)
dc.contributor.authorIllodo Brea, Sara
dc.date.accessioned2024-11-21T12:08:18Z
dc.date.available2024-11-21T12:08:18Z
dc.date.issued2024
dc.description.abstractNeurodegenerative diseases represent a major health problem. Biomolecules involved in these disorders are essential for life, but the misregulation of their interactions can lead to severe damage it. Thus, understanding these biomolecular interactions is vital for developing effective treatments. In this thesis, we study the self-assembly and binding processes of biomolecules like G-quadruplexes, amyloid peptides, and blood plasma proteins, which are thought to be involved in Alzheimer’s disease. Using microscopic and spectroscopic techniques, we study the mechanisms behind the selfassembly of G-Quadruplexes, the aggregation of amyloid peptides and the host-guest association of blood plasma proteins with fluorescence probes.
dc.description.programaUniversidade de Santiago de Compostela. Programa de Doutoramento en Ciencia e Tecnoloxía Química
dc.identifier.urihttps://hdl.handle.net/10347/37797
dc.language.isoeng
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International
dc.rights.accessRightsopen access
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectbiomolecules
dc.subjectself-assembly processes
dc.subjectSpectroscopic techniques
dc.subjectAlzheimer's disease (AD)
dc.subject.classification230221 Biología molecular
dc.subject.classification230112 Microscopia
dc.subject.classification230105 Espectroscopia de emisión
dc.titleStudy of biomolecular self-assembly and host-guest association using spectroscopic and microscopic techniques
dc.typedoctoral thesis
dspace.entity.typePublication
relation.isAdvisorOfPublication36dd13bf-de7b-4e4f-a7b2-ea620e7eafab
relation.isAdvisorOfPublication383c1bb0-bd2a-4f30-a468-590221b0a700
relation.isAdvisorOfPublication.latestForDiscovery36dd13bf-de7b-4e4f-a7b2-ea620e7eafab

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