Universitat de Lleida
    • English
    • català
    • español
  • English 
    • English
    • català
    • español
  • Login
Repositori Obert UdL
View Item 
  •   Home
  • Recerca
  • Química
  • Articles publicats (Química)
  • View Item
  •   Home
  • Recerca
  • Química
  • Articles publicats (Química)
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Hierarchical self-assembly of di-, tri- and tetraphenylalanine peptides capped with two fluorenyl functionalities: from polymorphs to dendrites

Thumbnail
View/Open
Postprint (1.424Mb)
Issue date
2016
Author
Mayans, Enric
Ballano, Gema
Casanovas Salas, Jordi
Valle, Luis J. del
Pérez-Madrigal, Maria M.
Estrany, Francesc
Jiménez, Ana I.
Puiggalí, Jordi
Cativiela, Carlos
Alemán, Carlos
Suggested citation
Mayans, Enric; Ballano, Gema; Casanovas Salas, Jordi; Valle, Luis J. del; Pérez-Madrigal, Maria M.; Estrany, Francesc; ... Alemán, Carlos. (2016) . Hierarchical self-assembly of di-, tri- and tetraphenylalanine peptides capped with two fluorenyl functionalities: from polymorphs to dendrites. Soft Matter, 2016, vol. 12, p. 5475-5488. https://doi.org/10.1039/C6SM00337K.
Impact


Web of Science logo    citations in Web of Science

Scopus logo    citations in Scopus

Google Scholar logo  Google Scholar
Share
Export to Mendeley
Metadata
Show full item record
Abstract
Homopeptides 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.
URI
http://hdl.handle.net/10459.1/65042
DOI
https://doi.org/10.1039/C6SM00337K
Is part of
Soft Matter, 2016, vol. 12, p. 5475-5488
European research projects
Collections
  • Articles publicats (Química) [313]
  • Publicacions de projectes de recerca del Plan Nacional [2956]

Contact Us | Send Feedback | Legal Notice
© 2023 BiD. Universitat de Lleida
Metadata subjected to 
 

 

Browse

All of the repositoryCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

Statistics

View Usage Statistics

D'interès

Política institucional d'accés obertDiposita les teves publicacionsDiposita dades de recercaSuport a la recerca

Contact Us | Send Feedback | Legal Notice
© 2023 BiD. Universitat de Lleida
Metadata subjected to