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Nematic and columnar ordering of a PEG-peptide conjugate in aqueous solution

Hamley, I.W., Krysmann, M.J., Castelletto, V., Kelarakis, A., Noirez, L., Hule, R.A. and Pochan, D.J. (2008) Nematic and columnar ordering of a PEG-peptide conjugate in aqueous solution. Chemistry- A European Journal, 14 (36). pp. 11369-11374. ISSN 0947-6539

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To link to this article DOI: 10.1002/chem.200800817

Abstract/Summary

The self-assembly in aqueous solution of a PEG-peptide conjugate is studied by spectroscopy, electron microscopy, rheology and small-angle Xray and neutron scattering (SAXS and SANS). The peptide fragment, FFKLVFF is based on fragment KLVFF of the amyloid beta-peptide, A beta(16-20), extended by two hydrophobic phenylalanine units. This is conjugated to PEG which confers water solubility and leads to distinct self-assembled structures. Small-angle scattering reveals the formation of cylindrical fibrils comprising a peptide core and PEG corona. This constrained structure leads to a model parallel beta-sheet self-assembled structure with a radial arrangement of beta sheets. Oil increasing concentration, successively nematic and hexagonal columnar phases are formed. The flow-induced alignment of both structures was studied in situ by SANS using a Couette cell. Shear-induced alignment is responsible for the shear thinning behaviour observed by dynamic shear rheometry. Incomplete recovery of moduli after cessation of shear is consistent with the observation from SANS of retained orientation in the sample.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:11313
Uncontrolled Keywords:amphiphiles, liquid crystals, peptides, polymer-peptide conjugates, self-assembly , PROTEIN SECONDARY STRUCTURE, SURFACTANT-LIKE PEPTIDES, HYBRID BLOCK-COPOLYMERS, AMPHIPHILE NANOFIBERS, PHASE-TRANSITIONS, FORM NANOTUBES, FIBRILS, BETA-AMYLOID(10-35), NANOVESICLES, ORGANIZATION

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