Self-assembly and gelation properties of glycine/leucine Fmoc-dipeptides

Claire Tang, Rein V. Ulijn, Alberto Saiani

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Self-assembly of aromatic peptide amphiphiles is known to be driven by a combination of π-π stacking of the aromatic moieties and hydrogen bonding between the peptide backbones, with possible stabilisation from the amino acid side chains. Phenylalanine-based Fmoc-dipeptides have previously been reported for their characteristic apparent pKa transitions, which were shown to coincide with significant structural and morphological changes that were peptide sequence dependent. Here, phenylalanine was replaced by leucine and the effect on the self-assembling behaviour of Fmoc-dipeptides was measured using potentiometry, fluorescence and infrared spectroscopy, transmission electron microscopy, X-ray scattering and shear rheometry. This study provides additional cues towards the elucidation of the sequence-structure relationship in self-assembling aromatic peptide amphiphiles. 

LanguageEnglish
Article number111
Number of pages11
JournalEuropean Physical Journal E
Volume36
Issue number10
DOIs
Publication statusPublished - 1 Oct 2013

Fingerprint

leucine
Dipeptides
gelation
Gelation
glycine
Leucine
Glycine
Self assembly
Peptides
peptides
self assembly
Amino acids
Amphiphiles
phenylalanine
assembling
Phenylalanine
Potentiometry
potentiometric analysis
Fluorescence Spectrometry
cues

Keywords

  • aromatic peptide amphiphiles
  • Fmoc-dipeptides
  • self-assembling behaviour of Fmoc-dipeptides

Cite this

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Self-assembly and gelation properties of glycine/leucine Fmoc-dipeptides. / Tang, Claire; Ulijn, Rein V.; Saiani, Alberto.

In: European Physical Journal E , Vol. 36, No. 10, 111, 01.10.2013.

Research output: Contribution to journalArticle

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