Journal article
Polymorphism in disease-related apolipoprotein C-II amyloid fibrils: a structural model for rod-like fibrils
CO Zlatic, Y Mao, N Todorova, YF Mok, GJ Howlett, I Yarovsky, PR Gooley, MDW Griffin
FEBS Journal | WILEY | Published : 2018
DOI: 10.1111/febs.14517
Abstract
Human apolipoprotein (apo) C-II is one of several plasma apolipoproteins that form amyloid deposits in vivo and is an independent risk factor for cardiovascular disease. Lipid-free apoC-II readily self-assembles into twisted-ribbon amyloid fibrils but forms straight, rod-like amyloid fibrils in the presence of low concentrations of micellar phospholipids. Charge mutations exerted significantly different effects on rod-like fibril formation compared to their effects on twisted-ribbon fibril formation. For instance, the double mutant, K30D-D69K apoC-II, readily formed twisted-ribbon fibrils, while the rate of rod-like fibril formation in the presence of micellar phospholipid was negligible. St..
View full abstractGrants
Awarded by National Computational Infrastructure
Funding Acknowledgements
MDWG is the recipient of an Australian Research Council Future Fellowship (project number FT140100544). IY and NT acknowledge the support from the NHMRC Centre of Research Excellence for Electromagnetic Bioeffects Research (CRE1042464). This research was undertaken with the assistance of resources from the National Computational Infrastructure (NCI, grant e87) and Melbourne Bioinformatics Facility, an initiative of the Victorian Government, Australia. Parts of this research were undertaken at the MX2 beam-line of the Australian Synchrotron, Victoria, Australia.