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dc.contributor.authorMartí Ballesté, Dídac
dc.contributor.authorMayans Tayadella, Enric
dc.contributor.authorGil, Ana M.
dc.contributor.authorDíaz Andrade, Angélica María
dc.contributor.authorJimenez Sanz, Ana Isabel
dc.contributor.authorYousef, Ibraheem
dc.contributor.authorKeridou, Ina
dc.contributor.authorCativiela, Carlos
dc.contributor.authorPuiggalí Bellalta, Jordi
dc.contributor.authorAlemán Llansó, Carlos
dc.contributor.otherUniversitat Politècnica de Catalunya. Departament d'Enginyeria Química
dc.date.accessioned2019-01-30T06:31:35Z
dc.date.available2019-12-18T01:25:52Z
dc.date.issued2018-11-19
dc.identifier.citationMartí, D. [et al.]. Amyloid-like fibrils from a diphenylalanine capped with an aromatic fluorenyl. "Langmuir", 19 Novembre 2018, vol. 34, núm. 50, p. 15551-15559.
dc.identifier.issn0743-7463
dc.identifier.urihttp://hdl.handle.net/2117/127843
dc.description.abstractThe self-assembly behavior of a diphenylalanine amphiphile blocked at the C-terminus with a 9-fluorenylmethyl ester and stabilized at the N-terminus with a trifluoroacetate (TFA) anion, TFA·FF-OFm, has been examined. At low peptide concentration (0.5 mg/mL), long amyloid-like fibrils, which come from the fusion of two or more helical ribbons and/or thinner fibrils, organized in bundles or as individual entities are detected. Microbeam synchrotron radiation infrared spectroscopy has shown that TFA·FF-OFm molecules in amyloid-like fibrils arrange, forming antiparallel ß-sheets. Alteration of the experimental conditions to prioritize the thermodynamic contribution with respect to the kinetic one in the self-assembly process inhibits the organization of amyloid-like structures in favor of the formation of conventional fibrous structures. On the basis of experimental observations, a structural model where the individual antiparallel ß-sheets are oriented in parallel has been proposed for TFA·FF-OFm amyloid-like fibrils.
dc.format.extent9 p.
dc.language.isoeng
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Spain
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
dc.subjectÀrees temàtiques de la UPC::Enginyeria química
dc.subject.lcshBiomedical materials
dc.subject.lcshPeptides
dc.titleAmyloid-like fibrils from a diphenylalanine capped with an aromatic fluorenyl
dc.typeArticle
dc.subject.lemacMaterials biomèdics
dc.subject.lemacPèptids
dc.contributor.groupUniversitat Politècnica de Catalunya. IMEM-BRT- Innovation in Materials and Molecular Engineering - Biomaterials for Regenerative Therapies
dc.contributor.groupUniversitat Politècnica de Catalunya. PSEP - Polimers Sintètics: Estructura i Propietats. Polimers Biodegradables.
dc.identifier.doi10.1021/acs.langmuir.8b03378
dc.description.peerreviewedPeer Reviewed
dc.relation.publisherversionhttps://pubs.acs.org/doi/10.1021/acs.langmuir.8b03378
dc.rights.accessOpen Access
local.identifier.drac23566178
dc.description.versionPostprint (author's final draft)
local.citation.authorMartí, D.; Mayans, E.; Gil, A.; Diaz, A.; Jimenez, A.; Yousef, I.; Keridou, I.; Cativiela, C.; Puiggali, J.; Aleman, C.
local.citation.publicationNameLangmuir
local.citation.volume34
local.citation.number50
local.citation.startingPage15551
local.citation.endingPage15559


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Except where otherwise noted, content on this work is licensed under a Creative Commons license : Attribution-NonCommercial-NoDerivs 3.0 Spain