Publication

Article Metrics

Citations


Online attention

Self-Assembly of PEGylated Peptide Conjugates Containing a Modified Amyloid beta-Peptide Fragment

DOI: 10.1021/la100110f DOI Help

Authors: V. Castelletto (University of Reading) , G. Newby (University of Reading) , Z. Zhu (Northwestern University) , I. W. Hamley (Diamond Light Source) , L. Noirez (CEA-CNRS Laboratoire Léon Brillouin)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Langmuir , VOL 26 (12) , PAGES 9986-9996

State: Published (Approved)
Published: January 2010

Abstract: The self-assembly of PEGylated peptides containing a modified sequence from the amyloid beta peptide, FEK LVFF, has been studied in aqueous solution. PEG molar masses PEG1k, PEG2k, and PEG10k were used in the conjugates. It is shown that the three FFK LVFF-PEG hybrids form fibrils comprising a FFKLVFF core and a PEG corona. The beta-sheet secondary structure of the peptide is retained in the FFK LVFF fibril core. At sufficiently high concentrations, FEK LVFF-PEG1k and FEK LVFF-PEG2k form a nema tic phase, while PEG10k-FEK LVFF exhibits a hexagonal columnar phase. Simultaneous small angle neutron scattering/shear flow experiments were performed to study the shear flow alignment of the nematic and hexagonal liquid crystal phases. On drying, PEG crystallization occurs without disruption of the FFK LVFF beta-sheet structure leading to characteristic peaks in the X-ray diffraction pattern and FTIR spectra. The stability of beta-sheet structures was also studied in blends of FFKLVFF-PEG conjugates with poly(acrylic acid) (PAA). While PEG crystallization is only observed up to 25% PAA content in the blends, the FFK LVFF beta-sheet structure is retained up to 75% PAA.

Subject Areas: Chemistry


Technical Areas:

Added On: 21/06/2010 14:18

Discipline Tags:



Technical Tags: