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

Pub. Date : 2009 Jul 16

PMID : 19537801






2 Functional Relationships(s)
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1 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)). 1,2-hexanoylphosphatidylcholine apolipoprotein C2 Homo sapiens
2 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)). 1,2-hexanoylphosphatidylcholine apolipoprotein C2 Homo sapiens