The effect of PEG crystallization on the morphology of PEG/peptide block copolymers containing amyloid β-peptide fragments

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Abstract

Ordered nanostructures are observed in the melt and solid state for a series of three peptide/ PEG conjugates containing fragments of amyloid β-peptides. These are conjugated to PEG with M̄n = 3300 g · mol-1 and a melting temperature Tm = 45-50 °C. The morphology at room temperature is examined by AFM and POM. This shows spherulite formation for the weakly fibrillizing KLVFF-PEG sample but fibril formation for FFKLVFF-PEG. The fibrillization tendency of the latter is enhanced by multiple phenylalanine residues. Simultaneous SAXS and WAXS was used to investigate the morphology as a function of temperature. The secondary structure is probed by FTIR. © 2008 WILEY-VCH Verlag GmbH & Co. KGaA,.

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Krysmann, M. J., Funari, S. S., Canetta, E., & Hamley, I. W. (2008). The effect of PEG crystallization on the morphology of PEG/peptide block copolymers containing amyloid β-peptide fragments. Macromolecular Chemistry and Physics, 209(9), 883–889. https://doi.org/10.1002/macp.200700605

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