ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2014
Copper-induced structural propensities of the amyloidogenic region of human prion protein.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- Prion therapeutics: Lessons from the past.Prion · 2022Review
- Using NMR spectroscopy to investigate the role played by copper in prion diseases.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2020Review
- Deciphering Copper Coordination in the Mammalian Prion Protein Amyloidogenic Domain.Biophysical journal · 2020Article
- Aggregation of biologically important peptides and proteins: inhibition or acceleration depending on protein and metal ion concentrations.RSC advances · 2019Review
- The Coordination Abilities of Three Novel Analogues of Saliva Peptides: The Influence of Structural Modification on the Copper Binding.International journal of peptide research and therapeutics · 2017Article
- In Absence of the Cellular Prion Protein, Alterations in Copper Metabolism and Copper-Dependent Oxidase Activity Affect Iron Distribution.Frontiers in neuroscience · 2016Article
- The non-octarepeat copper binding site of the prion protein is a key regulator of prion conversion.Scientific reports · 2015Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Transmissible spongiform encephalopathies are associated with the misfolding of the cellular Prion Protein (PrP(C)) to an abnormal protein isoform, called scrapie prion protein (PrP(Sc)). The structural rearrangement of the fragment of N-terminal domain of the protein spanning residues 91-127 is critical for the observed structural transition. The amyloidogenic domain of the protein encloses two copper-binding sites corresponding to His-96 and His-111 residues that act as anchors for metal ion binding. Previous studies have shown that Cu(II) sequestration by both sites may modulate the peptide's tendency to aggregation as it inflicts the hairpin-like structure that stabilizes the transition states leading to β-sheet formation. On the other hand, since both His sites differ in their ability to Cu(II) sequestration, with His-111 as a preferred binding site, we found it interesting to test the role of Cu(II) coordination to this single site on the structural properties of amyloidogenic domain. The obtained results reveal that copper binding to His-111 site imposes precise backbone bending and weakens the natural tendency of apo peptide to β-sheet formation.
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