ArticleProtein science : a publication of the Protein Society2014
Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 17 citations in OpenAlex.
- Thrombin-derived C-terminal peptides bind and form aggregates with sulfated glycosaminoglycans.Heliyon · 2024Article
- Amyloidogenic 60-71 deletion/ValThr insertion mutation of apolipoprotein A-I generates a new aggregation-prone segment that promotes nucleation through entropic effects.Scientific reports · 2023Article
- Thrombin-derived C-terminal fragments aggregate and scavenge bacteria and their proinflammatory products.The Journal of biological chemistry · 2020Article
- Probing the Basis of α-Synuclein Aggregation by Comparing Simulations to Single-Molecule Experiments.Biophysical journal · 2019Article
- Aggregation of thrombin-derived C-terminal fragments as a previously undisclosed host defense mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein A-I on Lipid Membranes.The Journal of biological chemistry · 2015Article
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
Several disease-linked mutations of apolipoprotein A-I, the major protein in high-density lipoprotein (HDL), are known to be amyloidogenic, and the fibrils often contain N-terminal fragments of the protein. Here, we present a combined computational and experimental study of the fibril-associated disordered 1-93 fragment of this protein, in wild-type and mutated (G26R, S36A, K40L, W50R) forms. In atomic-level Monte Carlo simulations of the free monomer, validated by circular dichroism spectroscopy, we observe changes in the position-dependent β-strand probability induced by mutations. We find that these conformational shifts match well with the effects of these mutations in thioflavin T fluorescence and transmission electron microscopy experiments. Together, our results point to molecular mechanisms that may have a key role in disease-linked aggregation of apolipoprotein A-I.
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