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Instruments / Technical Area	Publication Details	Published
	A thermoresponsive hydrogel based on telechelic PEG end-capped with hydrophobic dipeptides Ian W. Hamley , Ge Cheng , Valeria Castelletto Macromolecular Bioscience 11 (8) DOI: 10.1002/mabi.201100022 Show Abstract ▼ Abstract: The self-assembly in aqueous solution of PEG (1?500 Da) telechelically end-capped with hydrophobic dipeptides has been investigated using spectroscopic, microscopic, scattering, and rheological methods. A self-assembled ?-sheet fibril-based hydrogel has been identified (containing dityrosine end groups), which exhibits a gel–sol transition near body temperature. This thermo-responsive PEG-based biofunctional hydrogel is expected to have diverse potential uses in delivery or diagnostics for biomedical applications.	May 2011
B23-Circular Dichroism	Self-assembly of a modified amyloid peptide fragment: pH-responsiveness and nematic phase formation Ian W. Hamley , Valeria Castelletto , Claire Moulton , Daniel Myatt , Guiliano Siligardi , Cristiano L. P. Oliveira , Jan Skov Pederson , Inbal Abutbul , Dganit Danino Macromolecular Bioscience 10, 40 - 48 DOI: 10.1002/mabi.200900217 Show Abstract ▼ Abstract: The self-assembly of peptide YYKLVFFC based on a fragment of the amyloid beta (Aβ) peptide, Aβ16–20, KLVFF has been studied in aqueous solution. The peptide is designed with multiple functional residues to examine the interplay between aromatic interactions and charge on the self-assembly, as well as specific transformations such as the pH-induced phenol–phenolate transition of the tyrosine residue. Circular dichroism (CD) and Fourier-transform infrared (FTIR) spectroscopies are used to investigate the conditions for β-sheet self-assembly and the role of aromatic interactions in the CD spectrum as a function of pH and concentration. The formation of well-defined fibrils at pH 4.7 is confirmed by cryo-TEM (transmission electron microscope) and negative stain TEM. The morphology changes at higher pH, and aggregates of short twisted fibrils are observed at pH 11. Polarized optical microscopy shows birefringence at a low concentration (1 wt.-%) of YYKLVFFC in aqueous solution, and small-angle X-ray scattering was used to probe nematic phase formation in more detail. A pH-induced transition from nematic to isotropic phases is observed on increasing pH that appears to be correlated to a reduction in aggregate anisotropy upon increasing pH.	Sep 2009
NONE-No attached Diamond beamline	Interactions of KLVFF-PEG peptide with fibrinogen in neutral aqueous solutions Valerie Castelletto , Ian W. Hamley , Gemma E. Newby Macromolecular Bioscience 8 (12), 1182-1189 DOI: 10.1002/mabi.200800065 Show Abstract ▼ Abstract: In this work we report on the interaction of KLVFF-PEG with fibrinogen (Fbg) in neutral aqueous solutions at 20 °C, for particular ratios of KLVFF-PEG to Fbg concentration, Δ = cKLVFF-PEG/cFbg. Our results show the formation of Fbg/KLVFF-PEG complexes for Δ > 0, such that there is not an extended network of complexes throughout the solution. In addition, cleaved protein and Fbg dimers are identified in the solution for Δ ≥ 0. There is a dramatic change in the tertiary structure of the Fbg upon KLVFF-PEG binding, although the KLVFF-PEG binds to the Fbg without affecting the secondary structure elements of the glycoprotein.	Jun 2008

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