Jump to main content
Jump to site search

Issue 4, 2010
Previous Article Next Article

Self-assembly of an amyloid peptide fragment–PEG conjugate: lyotropic phase formation and influence of PEG crystallization

Author affiliations

Abstract

The self-assembly of PEGylated peptides containing a modified sequence from the amyloid β peptide, YYKLVFF, has been studied in aqueous solution. Two PEG molar masses, PEG1k and PEG3k, were used in the conjugates. It is shown that both YYKLVFF–PEG hybrids form fibrils comprising a peptide core and a PEG corona. The fibrils are much longer for YYKLVFF–PEG1k, pointing to an influence of PEG chain length. The β-sheet secondary structure of the peptide is retained in the conjugate. Lyotropic liquid crystal phases, specifically nematic and hexagonal columnar phases, are formed at sufficiently high concentration. Flow alignment of these mesophases was investigated by small-angle neutron scattering with in situ steady shearing in a Couette cell. On drying, PEG crystallization occurs leading to characteristic peaks in the X-ray diffraction pattern, and to lamellar structures imaged by atomic force microscopy. The X-ray diffraction pattern retains features of the cross-β pattern from the β-sheet structure, showing that this is not disrupted by PEG crystallization.

Graphical abstract: Self-assembly of an amyloid peptide fragment–PEG conjugate: lyotropic phase formation and influence of PEG crystallization

Back to tab navigation

Article information


Submitted
13 Nov 2009
Accepted
20 Dec 2009
First published
01 Feb 2010

Polym. Chem., 2010,1, 453-459
Article type
Paper

Self-assembly of an amyloid peptide fragment–PEG conjugate: lyotropic phase formation and influence of PEG crystallization

V. Castelletto, G. E. Newby, D. Hermida Merino, I. W. Hamley, D. Liu and L. Noirez, Polym. Chem., 2010, 1, 453
DOI: 10.1039/B9PY00349E

Social activity

Search articles by author

Spotlight

Advertisements