Journal article
Effects of mutation on the amyloidogenic propensity of apolipoprotein C-II60-70 peptide
N Todorova, A Hung, SM Maaser, MDW Griffin, J Karas, GJ Howlett, I Yarovsky
Physical Chemistry Chemical Physics | ROYAL SOC CHEMISTRY | Published : 2010
DOI: 10.1039/c0cp00299b
Abstract
Using experimental and computational methods we identified the effects of mutation on the structure and dynamics of the amyloidogenic peptide apoC-II(60-70), in monomeric and oligomeric states. Methionine (Met60) substitutions to hydrophilic Gln, hydrophobic Val, and methionine sulfoxide residues were investigated and the results compared with observations of fibril formation by the wild-type, Met60Gln, Met60Val, and oxidised Met60 (oxi-Met) apoC-II(60-70) peptides. ThT fluorescence measurements showed fibril formation by all peptides, however with different kinetics. The wild-type and Met60Val peptides formed fibrils fastest, while oxi-Met and Met60Gln peptides exhibited significantly longe..
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Awarded by Australian Research Council
Funding Acknowledgements
The authors would like to thank the Australian Research Council for providing funding for the project (DP0984565). The Australian National Computational Infrastructure (NCI) and Victorian Partnership for Advanced Computing (VPAC) for providing the computational resources. We also acknowledge our colleagues Sue Legge and Katrina Binger for useful discussions.