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Effect of PEG Crystallization on the Self-Assembly of PEG/Peptide Copolymers Containing Amyloid Peptide Fragments

DOI: 10.1021/la8005426 DOI Help
PMID: 18598063 PMID Help

Authors: M.j. Krysmann (University of Reading) , Ian Hamley (Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Langmuir , VOL 24 (15) , PAGES 8210-8214

State: Published (Approved)
Published: August 2008

Abstract: The effect of poly(ethylene glycol) PEG crystallization on P-sheet fibril formation is studied for a series of three peptide/PEG conjugates containing fragments modified from the amyloid P peptide, specifically KLVFF, FFKLVFF, and AAKLVFF. These are conjugated to PEG with M-n = 3300 g mol(-1). It is found, via small-angle X-ray scattering,X-ray diffraction, atomic force microscopy, and polarized optical microscopy, that PEG crystallinity in dried samples can disturb fibrillization, in particular cross-P amyloid structure formation, for the conjugate containing the weak fibrillizer KLVFF, whereas this is retained for the conjugates containing the stronger fibrillizers AAKLVFF and FFKLVFF. For these two samples, the alignment of peptide fibrils also drives the orientation of the attached PEG chains. Our results highlight the importance of the antagonistic effects of PEG crystallization and peptide fibril formation in PEG/peptide conjugates.

Subject Areas: Chemistry, Materials

Instruments: NONE-No attached Diamond beamline

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