Heterochirality Restricts the Self-Assembly of Phenylalanine Dipeptides Capped with Highly Aromatic Groups

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dc.contributor.authorGil, Ana M.
dc.contributor.authorCasanovas Salas, Jordi
dc.contributor.authorMayans, Enric
dc.contributor.authorJiménez, Ana I.
dc.contributor.authorPuiggalí, Jordi
dc.contributor.authorAlemán, Carlos
dc.date.accessioned2022-02-17T12:06:44Z
dc.date.available2022-02-17T12:06:44Z
dc.date.issued2020
dc.description.abstractThe influence of stereochemistry on the self-assembly of phenylalanine (Phe) dipeptides bearing aromatic fluorenyl groups at both the N- and C-termini (Fmoc, OFm) has been investigated. For this purpose, Fmoc–d-Phe–l-Phe–OFm and Fmoc–l-Phe–l-Phe–OFm have been examined considering a wide variety of solvents, which differ in dielectric constant and volatility. Results reveal that replacement of l-Phe by d-Phe has a major impact on the self-assembly propensities, restricting drastically the structural diversity and polymorphism shown by the homochiral dipeptide. Thus, the analogous heterochiral dipeptide shows a great propensity to form micro/nanofibers, independently of the environmental conditions. Theoretical calculations revealed that the stability of antiparallel disposition is much higher (a factor of ca. 15) for Fmoc–d-Phe–l-Phe–OFm than that for Fmoc–l-Phe–l-Phe–OFm, which has been attributed to the hydrophobic core formed in the former. Overall, results suggest that control of the backbone chirality is a potent and versatile strategy to drive and finely tune the self-assembly propensities of highly aromatic peptides.ca_ES
dc.description.sponsorshipThis work was supported by MINECO (RTI2018-098951-B-I00, RTI2018-101827-B-I00, and CTQ2013-40855-R), AGAUR (2017SGR359 and 2017SGR373), and Gobierno de Aragon (research group Aminoacidos y Peptidos E19_20R). 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.identifier.doihttps://doi.org/10.1021/acs.jpcb.0c04513
dc.identifier.idgrec030346
dc.identifier.issn1520-6106
dc.identifier.urihttp://hdl.handle.net/10459.1/73027
dc.language.isoengca_ES
dc.publisherAmerican Chemical Societyca_ES
dc.relationinfo:eu-repo/grantAgreement/MINECO//CTQ2013-40855-R/ES/AMINOACIDOS NO PROTEICOS Y DERIVADOS PARA APLICACIONES EN AGROQUIMICA Y BIOMEDICINA/ca_ES
dc.relation.isformatofVersió acceptada del document publicat a https://doi.org/10.1021/acs.jpcb.0c04513ca_ES
dc.relation.ispartofJournal of Physical Chemistry B, 2020, vol. 124, núm. 28, p. 5913-5918ca_ES
dc.rights(c) American Chemical Society, 2020ca_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessca_ES
dc.subjectChemical structureca_ES
dc.subjectSelf organizationca_ES
dc.subjectAromatic compoundsca_ES
dc.subjectPeptides and proteinsca_ES
dc.titleHeterochirality Restricts the Self-Assembly of Phenylalanine Dipeptides Capped with Highly Aromatic Groupsca_ES
dc.typeinfo:eu-repo/semantics/articleca_ES
dc.type.versioninfo:eu-repo/semantics/acceptedVersionca_ES
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