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

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Krysmann, M.J., Funari, S.S., Canetta, E. and Hamley, I.W. ORCID: https://orcid.org/0000-0002-4549-0926 (2008) The effect of PEG crystallization on the morphology of PEG/peptide block copolymers containing amyloid beta-peptide fragments. Macromolecular Chemistry and Physics, 209 (9). pp. 883-889. ISSN 1022-1352

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To link to this item DOI: 10.1002/macp.200700605

Abstract/Summary

Ordered nanostructures are observed in the melt and solid state for a series of three peptide/PEG conjugates containing fragments of amyloid beta-peptides. These are conjugated to PEG with (M) over bar (n) = 3 300 g.mol(-1) and a melting temperature T-m = 45-50 degrees 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.

Item Type:Article
Refereed:Yes
Divisions:Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:11411
Uncontrolled Keywords:block copolymers, microstructure, peptides, small-angle X-ray scattering (SAXS) , POLY(ETHYLENE GLYCOL), ALZHEIMERS-DISEASE, FIBRIL FORMATION, PROTEINS, FIBRILLOGENESIS, BETA-AMYLOID(10-35), SPECTROSCOPY, POLYMERS, CHAINS
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