Self assembly of a model amphiphilic phenylalanine peptide/polyethylene glycol block copolymer in aqueous solution.
Puroindoline-a, a lipid binding protein from common wheat, spontaneously forms prolate protein micelles in solution.
- L. Clifton, M. Sanders, R. J. Green
- Chemistry, BiologyPhysical Chemistry, Chemical Physics - PCCP
- 27 April 2011
Pin-a micelles could be disrupted upon addition of the non-ionic surfactant dodecyl-β-maltoside, suggesting that the protein self-assembly is driven by hydrophobic forces, consisting of intermolecular interactions between Trp residues located within a well-defined Trp-rich domain of Pin-a.
Toll-like receptor agonist lipopeptides self-assemble into distinct nanostructures.
- I. Hamley, S. Kirkham, A. Dehsorkhi, V. Castelletto, M. Reza, J. Ruokolainen
- Chemistry, BiologyChemical Communications
- 20 November 2014
The self-assembled structure of toll-like receptor agonist lipopeptides containing the CSK4 peptide sequence is examined in aqueous solution. A remarkable dependence of morphology on the number of…
Fibrillisation of hydrophobically modified amyloid peptide fragments in an organic solvent.
UV fluorescence experiments on unstained peptide and CD point to the importance of aromatic interactions between phenylalanine groups in driving aggregation into β-sheets and FTIR suggests that aggregation occurs at low concentration and is not strongly affected by further increase in concentration.
Effect of Sequence Distribution on the Morphology, Crystallization, Melting, and Biodegradation of Poly(ε-caprolactone-co-ε-caprolactam) Copolymers
- R. M. Michell, A. Müller, V. Castelletto, I. Hamley, Gaëlle Deshayes, P. Dubois
- Materials Science
- 10 August 2009
Two types of poly(e-caprolactone (CLo))-co-poly(e-caprolactam (CLa)) copolymers were prepared by catalyzed hydrolytic ring-opening polymerization. Both cyclic comonomers were added simultaneously in…
Self-assembling amphiphilic peptides†
The self‐assembly of several classes of amphiphilic peptides is reviewed, and selected applications are discussed, and the influence of environmental variables such as pH and temperature on aggregate nanostructure is discussed.
Self-assembly and hydrogelation of an amyloid peptide fragment.
- M. Krysmann, V. Castelletto, A. Kelarakis, I. Hamley, Rohan A. Hule, D. Pochan
- Materials ScienceBiochemistry
- 28 March 2008
In dilute solution, self-assembly of NH 2-KLVFF-COOH is strongly influenced by aromatic interactions between phenylalanine units, as revealed by UV spectroscopy and circular dichroism, and X-ray diffraction and cryo-TEM provide further support for beta-sheet amyloid fibril formation.
Low-molecular-weight gelators: elucidating the principles of gelation based on gelator solubility and a cooperative self-assembly model.
- Andrew R. Hirst, I. Coates, David K. Smith
- Materials ScienceJournal of the American Chemical Society
- 18 June 2008
This paper relates thermal stability and minimum gelation concentration values of small-molecule gelation in terms of the solubility and cooperative self-assembly of gelator building blocks and reports that the critical concentration of gelators incorporated into the solid-phase sample-spanning network within the gel is invariant of Gelator structural design.
Direct observation of time-resolved polymorphic states in the self-assembly of end-capped heptapeptides.
- J. Adamcik, V. Castelletto, S. Bolisetty, I. Hamley, R. Mezzenga
- Biology, Materials ScienceAngewandte Chemie
- 6 June 2011
Understanding the mechanism of amyloid fibril formation can improve strategies towards the prevention of fibrillation processes and enable a wide range of potential applications in nanotemplating and nanotechnology.