Journal article
NBD-labeled phospholipid accelerates apolipoprotein C-II amyloid fibril formation but is not incorporated into mature fibrils
TM Ryan, MDW Griffin, MF Bailey, P Schuck, GJ Howlett
Biochemistry | AMER CHEMICAL SOC | Published : 2011
DOI: 10.1021/bi201192r
Abstract
Human apolipoprotein (apo) C-II is one of several lipid-binding proteins that self-assemble into fibrils and accumulate in disease-related amyloid deposits. A general characteristic of these amyloid deposits is the presence of lipids, known to modulate individual steps in amyloid fibril formation. ApoC-II fibril formation is activated by submicellar phospholipids but inhibited by micellar lipids. We examined the mechanism for the activation by submicellar lipids using the fluorescently labeled, short-chain phospholipid 1-dodecyl-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]-2-hydroxyglycero-3- phosphocholine (NBD-lyso-12-PC). Addition of submicellar NBD-lyso-12-PC increased the rate of fibril fo..
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Awarded by National Institute of Biomedical Imaging and Bioengineering
Funding Acknowledgements
This research was supported under the Australian Research Council's Discovery Projects funding scheme (Project DP0984565). M.D.W.G. is the recipient of an Australian Research Council Post Doctoral Fellowship (Project DP110103528). This work was supported in part by the Intramural Research Program of the National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health.