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Twisted nanoribbons from a RGD-bearing cholic acid derivative

Travaglini, Leana; Giordano, Cesare; D'Annibale, Andrea; Gubitosi, Marta LU ; di Gregorio, Maria Chiara; Schillén, Karin LU ; Stefanucci, Azzurra; Mollica, Adriano; Pavel, Nicolae Viorel and Galantini, Luciano (2017) In Colloids and Surfaces B: Biointerfaces 159. p.183-190
Abstract

In light of the biomedical interest for self-assembling amphiphiles bearing the tripeptide Arg-Gly-Gly (RGD), a cholic acid derivative was synthesized by introducing an aromatic moiety on the steroidal skeleton and the RGD sequence on the carboxylic function of its chain 17–24, thus forming a peptide amphiphile with the unconventional rigid amphiphilic structure of bile salts. In aqueous solution, the compound self-assembled into long twisted ribbons characterized by a very low degree of polydispersity in terms of width (≈25 nm), thickness (≈4.5 nm) and pitch (≈145 nm). It was proposed that in the ribbon the molecules are arranged in a bilayer structure with the aromatic moieties in the interior, strongly involved in the intermolecular... (More)

In light of the biomedical interest for self-assembling amphiphiles bearing the tripeptide Arg-Gly-Gly (RGD), a cholic acid derivative was synthesized by introducing an aromatic moiety on the steroidal skeleton and the RGD sequence on the carboxylic function of its chain 17–24, thus forming a peptide amphiphile with the unconventional rigid amphiphilic structure of bile salts. In aqueous solution, the compound self-assembled into long twisted ribbons characterized by a very low degree of polydispersity in terms of width (≈25 nm), thickness (≈4.5 nm) and pitch (≈145 nm). It was proposed that in the ribbon the molecules are arranged in a bilayer structure with the aromatic moieties in the interior, strongly involved in the intermolecular interaction, whereas the RGD residues are located at the bilayer-water interface. The nanostructure is significantly different from those generally provided by RGD-containing amphiphiles with the conventional peptide-tail structure, for which fibers with a circular cross-section were observed, and successfully tested as scaffolds for tissue regeneration. From previous work on the use of this kind of nanostructures, it is known that features like morphology, rigidity, epitope spacing and periodicity are important factors that dramatically affect cell adhesion and signaling. Within this context, the reported results demonstrate that bile salt-based peptide surfactants are promising building blocks in the preparation of non-trivial RGD-decorated nanoaggregates with well-defined morphologies and epitope distributions.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Bile acids, RGD amphiphiles, Self-assembly, Supramolecular nanoribbons
in
Colloids and Surfaces B: Biointerfaces
volume
159
pages
8 pages
publisher
Elsevier
external identifiers
  • scopus:85026738607
  • wos:000418729600022
ISSN
0927-7765
DOI
10.1016/j.colsurfb.2017.07.084
language
English
LU publication?
yes
id
49fefe66-abdb-4d84-8be8-7a2eb7ed2a30
date added to LUP
2017-08-25 11:12:01
date last changed
2018-01-16 13:23:32
@article{49fefe66-abdb-4d84-8be8-7a2eb7ed2a30,
  abstract     = {<p>In light of the biomedical interest for self-assembling amphiphiles bearing the tripeptide Arg-Gly-Gly (RGD), a cholic acid derivative was synthesized by introducing an aromatic moiety on the steroidal skeleton and the RGD sequence on the carboxylic function of its chain 17–24, thus forming a peptide amphiphile with the unconventional rigid amphiphilic structure of bile salts. In aqueous solution, the compound self-assembled into long twisted ribbons characterized by a very low degree of polydispersity in terms of width (≈25 nm), thickness (≈4.5 nm) and pitch (≈145 nm). It was proposed that in the ribbon the molecules are arranged in a bilayer structure with the aromatic moieties in the interior, strongly involved in the intermolecular interaction, whereas the RGD residues are located at the bilayer-water interface. The nanostructure is significantly different from those generally provided by RGD-containing amphiphiles with the conventional peptide-tail structure, for which fibers with a circular cross-section were observed, and successfully tested as scaffolds for tissue regeneration. From previous work on the use of this kind of nanostructures, it is known that features like morphology, rigidity, epitope spacing and periodicity are important factors that dramatically affect cell adhesion and signaling. Within this context, the reported results demonstrate that bile salt-based peptide surfactants are promising building blocks in the preparation of non-trivial RGD-decorated nanoaggregates with well-defined morphologies and epitope distributions.</p>},
  author       = {Travaglini, Leana and Giordano, Cesare and D'Annibale, Andrea and Gubitosi, Marta and di Gregorio, Maria Chiara and Schillén, Karin and Stefanucci, Azzurra and Mollica, Adriano and Pavel, Nicolae Viorel and Galantini, Luciano},
  issn         = {0927-7765},
  keyword      = {Bile acids,RGD amphiphiles,Self-assembly,Supramolecular nanoribbons},
  language     = {eng},
  month        = {11},
  pages        = {183--190},
  publisher    = {Elsevier},
  series       = {Colloids and Surfaces B: Biointerfaces},
  title        = {Twisted nanoribbons from a RGD-bearing cholic acid derivative},
  url          = {http://dx.doi.org/10.1016/j.colsurfb.2017.07.084},
  volume       = {159},
  year         = {2017},
}