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dc.contributor.authorMayans, Enric
dc.contributor.authorBallano, Gema
dc.contributor.authorCasanovas Salas, Jordi
dc.contributor.authorValle, Luis J. del
dc.contributor.authorPérez-Madrigal, Maria M.
dc.contributor.authorEstrany, Francesc
dc.contributor.authorJiménez, Ana I.
dc.contributor.authorPuiggalí, Jordi
dc.contributor.authorCativiela, Carlos
dc.contributor.authorAlemán, Carlos
dc.date.accessioned2018-11-07T10:26:03Z
dc.date.available2018-11-07T10:26:03Z
dc.date.issued2016
dc.identifier.issn1744-6848
dc.identifier.urihttp://hdl.handle.net/10459.1/65042
dc.description.abstractHomopeptides with 2, 3 and 4 phenylalanine (Phe) residues and capped with fluorenylmethoxycarbonyl and fluorenylmethyl esters at the N-terminus and C-terminus, respectively, have been synthesized to examine their self-assembly capabilities. Depending on the conditions, the di- and triphenylalanine derivatives self-organize into a wide variety of stable polymorphic structures, which have been characterized: stacked braids, doughnut-like shapes, bundled arrays of nanotubes, corkscrew-like shapes and spherulitic microstructures. These highly aromatic Phe-based peptides also form incipient branched dendritic microstructures, even though they are highly unstable, making their manipulation very difficult. Conversely, the tetraphenylalanine derivative spontaneously self-assembles into stable dendritic microarchitectures made of branches growing from nucleated primary frameworks. The fractal dimension of these microstructures is ∼1.70, which provides evidence for self-similarity and two-dimensional diffusion controlled growth. DFT calculations at the M06L/6-31G(d) level have been carried out on model β-sheets since this is the most elementary building block of Phe-based peptide polymorphs. The results indicate that the antiparallel β-sheet is more stable than the parallel one, with the difference between them growing with the number of Phe residues. Thus, the cooperative effects associated with the antiparallel disposition become more favorable when the number of Phe residues increases from 2 to 4, while those of the parallel disposition remained practically constant.ca_ES
dc.description.sponsorshipThe authors thank the support from MINECO and FEDER (MAT2012-34498, MAT2012-36205 and CTQ2013-40855-R), Generalitat de Catalunya (XRQTC) and CESCA and Gobierno de Aragón – Fondo Social Europeo (research group E40). Support for the research of C. A. was received through the prize ‘‘ICREA Academia’’ for excellence in research funded by the Generalitat de Catalunya.ca_ES
dc.language.isoengca_ES
dc.publisherRoyal Society of Chemistryca_ES
dc.relationMICINN/PN2008-2011/MAT2012-34498
dc.relationMICINN/PN2008-2011/MAT2012-36205
dc.relationMINECO/PN2013-2016/CTQ2013-40855-R
dc.relation.isformatofVersió postprint del document publicat a https://doi.org/10.1039/C6SM00337Kca_ES
dc.relation.ispartofSoft Matter, 2016, vol. 12, p. 5475-5488ca_ES
dc.rights(c) Royal Society of Chemistry, 2016ca_ES
dc.titleHierarchical self-assembly of di-, tri- and tetraphenylalanine peptides capped with two fluorenyl functionalities: from polymorphs to dendritesca_ES
dc.typeinfo:eu-repo/semantics/articleca_ES
dc.identifier.idgrec023987
dc.type.versioninfo:eu-repo/semantics/acceptedVersionca_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessca_ES
dc.identifier.doihttps://doi.org/10.1039/C6SM00337K


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