Self-Assembly of Tetraphenylalanine Peptides

Three different tetraphenylalanine (FFFF) based peptides that differ at the N‐ and C‐termini have been synthesized by using standard procedures to study their ability to form different nanoassemblies under a variety of conditions. The FFFF peptide assembles into nanotubes that show more structural i...

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Bibliographic Details
Published in:Chemistry : a European journal 2015-11, Vol.21 (47), p.16895-16905
Main Authors: Mayans , Enric, Ballano, Gema, Casanovas, Jordi, Díaz , Angélica, Pérez-Madrigal , Maria M., Estrany, Francesc, Puiggalí , Jordi, Cativiela, Carlos, Alemán , Carlos
Format: Article
Language:English
Subjects:
Assembly
beta sheet
Chemistry
Enginyeria química
Esters
Fluorenes - chemistry
hydrogen bonds
Mathematical models
Molecular Dynamics Simulation
Nanostructure
Nanotubes
Nanotubes - chemistry
Peptides
Peptides - chemical synthesis
Peptides - chemistry
phenylalanine
Phenylalanine - analogs & derivatives
Phenylalanine - chemical synthesis
Phenylalanine - chemistry
pi interactions
Pèptids
Self assembly
Àrees temàtiques de la UPC
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Summary:Three different tetraphenylalanine (FFFF) based peptides that differ at the N‐ and C‐termini have been synthesized by using standard procedures to study their ability to form different nanoassemblies under a variety of conditions. The FFFF peptide assembles into nanotubes that show more structural imperfections at the surface than those formed by the diphenylalanine (FF) peptide under the same conditions. Periodic DFT calculations (M06L functional) were used to propose a model that consists of three FFFF molecules defining a ring through head‐to‐tail NH3+⋅⋅⋅−OOC interactions, which in turn stack to produce deformed channels with internal diameters between 12 and 16 Å. Depending on the experimental conditions used for the peptide incubation, N‐fluorenylmethoxycarbonyl (Fmoc) protected FFFF self‐assembles into a variety of polymorphs: ultra‐thin nanoplates, fibrils, and star‐like submicrometric aggregates. DFT calculations indicate that Fmoc‐FFFF prefers a parallel rather than an antiparallel β‐sheet assembly. Finally, coexisting multiple assemblies (up to three) were observed for Fmoc‐FFFF‐OBzl (OBzl = benzyl ester), which incorporates aromatic protecting groups at the two peptide terminals. This unusual and noticeable feature is attributed to the fact that the assemblies obtained by combining the Fmoc and OBzl groups contained in the peptide are isoenergetic. Variety show! Three different tetraphenylalanine‐based peptides that differ at the N‐ and C‐termini have been synthesized by using standard procedures to study their ability to form different nanoassemblies (e.g., nanotubes, see figure) under a variety of conditions.
ISSN:0947-6539
1521-3765
1521-3765
DOI:10.1002/chem.201501793