Lipids enhance apolipoprotein C-II-derived amyloidogenic peptide oligomerization but inhibit fibril formation.

@article{Hung2009LipidsEA,
  title={Lipids enhance apolipoprotein C-II-derived amyloidogenic peptide oligomerization but inhibit fibril formation.},
  author={Andrew Hung and Michael D. W. Griffin and Geoffrey J. Howlett and Irene Yarovsky},
  journal={The journal of physical chemistry. B},
  year={2009},
  volume={113 28},
  pages={
          9447-53
        }
}
We investigated the effect of submicellar lipids on amyloid fibril formation. Thioflavin T fluorescence studies showed that submicellar levels of the short-chain phospholipids, dipentanoylphosphatidylcholine and dihexanoylphosphatidylcholine, strongly inhibited amyloid fibril formation by an 11-residue peptide derived from human apolipoprotein C-II (apoC-II(60-70)). In contrast, sedimentation equilibrium analysis of these peptide-lipid mixtures indicated the presence of soluble oligomeric… Expand
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