ArticleBiophysical journal2006
Natively folded HypF-N and its early amyloid aggregates interact with phospholipid monolayers and destabilize supported phospholipid bilayers.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Toxic oligomers of the amyloidogenic HypF-N protein form pores in mitochondrial membranes.Scientific reports · 2020Article
- The Amphipathic GM1 Molecule Stabilizes Amyloid Aggregates, Preventing their Cytotoxicity.Biophysical journal · 2020Article
- Amyloidogenic Peptides in Human Neuro-Degenerative Diseases and in Microorganisms: A Sorrow Shared Is a Sorrow Halved?Molecules (Basel, Switzerland) · 2020Review
- Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers.Biomolecular NMR assignments · 2018Article
- Interaction of toxic and non-toxic HypF-N oligomers with lipid bilayers investigated at high resolution with atomic force microscopy.Oncotarget · 2016Article
- Organized films.Beilstein journal of nanotechnology · 2016Article
- Misfolding of amyloidogenic proteins and their interactions with membranes.Biomolecules · 2013Review
- α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling.The Journal of biological chemistry · 2013Article
- The γ-secretase blocker DAPT reduces the permeability of the blood-brain barrier by decreasing the ubiquitination and degradation of occludin during permanent brain ischemia.CNS neuroscience & therapeutics · 2013Article
- Article
- A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells.Journal of cellular and molecular medicine · 2011Article
- Thermodynamics of monolayers formed by mixtures of phosphatidylcholine/phosphatidylserine.Colloids and surfaces. B, Biointerfaces · 2011Article
- Components of the E. coli envelope are affected by and can react to protein over-production in the cytoplasm.Microbial cell factories · 2009Article
- Nonspecific interaction of prefibrillar amyloid aggregates with glutamatergic receptors results in Ca2+ increase in primary neuronal cells.The Journal of biological chemistry · 2008Article
- Acridine derivatives inhibit lysozyme aggregation.European biophysics journal : EBJ · 2008Article
- Nanoparticles as catalysts for protein fibrillation.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent data depict membranes as the main sites where proteins/peptides are recruited and concentrated, misfold, and nucleate amyloids; at the same time, membranes are considered key triggers of amyloid toxicity. The N-terminal domain of the prokaryotic hydrogenase maturation factor HypF (HypF-N) in 30% trifluoroethanol undergoes a complex path of fibrillation starting with initial 2-3-nm oligomers and culminating with the appearance of mature fibrils. Oligomers are highly cytotoxic and permeabilize lipid membranes, both biological and synthetic. In this article, we report an in-depth study aimed at providing information on the surface activity of HypF-N and its interaction with synthetic membranes of different lipid composition, either in the native conformation or as amyloid oligomers or fibrils. Like other amyloidogenic peptides, the natively folded HypF-N forms stable films at the air/water interface and inserts into synthetic phospholipid bilayers with efficiencies depending on the type of phospholipid. In addition, HypF-N prefibrillar aggregates interact with, insert into, and disassemble supported phospholipid bilayers similarly to other amyloidogenic peptides. These results support the idea that, at least in most cases, early amyloid aggregates of different peptides and proteins produce similar effects on the integrity of membrane assembly and hence on cell viability.
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