Influence of divalent copper, manganese and zinc ions on fibril nucleation and elongation of the amyloid-like yeast prion determinant Sup35p-NM

Suhre, Michael H.; Heß, Simone; Golser, Adrian V.; Scheibel, Thomas

doi:10.1016/j.jinorgbio.2009.09.021

Cited by 12 publications

(8 citation statements)

References 81 publications

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“…Cross-seeding of various proteins with eADF4(C16) particles Previously, it has been shown that structure-related cross-seeding of protein fibrils was possible using different protein variants or even unrelated proteins (Jayaraman et al, 2009;O'Nuallain et al, 2004). In order to test if the observed seeding effect of the particles was sequence or structure specific, the related spider silk protein eADF3(AQ)12 (Huemmerich et al, 2004), unable to fibrilize, and amylogenic Sup35p-NM (Krammer et al, 2009;Scheibel and Lindquist, 2001;Slotta et al, 2007;Suhre et al, 2009), with no sequence similarity to spider silk proteins, were tested. eADF3(AQ)12 did not form cross-b fibrils in presence of eADF4(16) particles, whereas the ability of Sup35p-NM to self-assemble into cross-b fibrils persisted.…”

Section: Nucleation Interfaces Triggering Eadf4(c16) Fibril Assemblymentioning

confidence: 99%

Ion and seed dependent fibril assembly of a spidroin core domain

Humeník

Smith

Arndt

et al. 2015

Journal of Structural Biology

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Section: Nucleation Interfaces Triggering Eadf4(c16) Fibril Assemblymentioning

confidence: 99%

Ion and seed dependent fibril assembly of a spidroin core domain

Humeník

Smith

Arndt

et al. 2015

Journal of Structural Biology

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“…In 2009 we identified more than 400 articles after searching Web of Science, PubMed, SciDir and OVID databases using ‘isothermal AND titration AND calorimetry’ or ITC or ‘Isothermal Titration Calorimetry’ search terms. These have been classified into the following categories: Pre‐2009 references cited in the text and review articles 1–43 Protein‐protein and protein‐peptide interactions 44–124 Protein/peptide‐small molecule interactions 125–218 Protein/peptide‐metal ion interactions 219–253 Protein/peptide‐nucleic acid interactions 254–273 Protein/peptide‐lipid interactions 274–292 Protein/peptide‐polysaccharide interactions 293–316 Nucleic acid‐small molecule interactions 317–348 Small molecule interactions …”

Section: Introductionmentioning

confidence: 99%

Survey of the year 2009: applications of isothermal titration calorimetry

Falconer

Collins

2010

J. Mol. Recognit.

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Isothermal titration calorimetry (ITC) is now an established and invaluable method for determining the thermodynamic constants, association constant and stoichiometry of molecular interactions in aqueous solutions. The technique has become widely used by biochemists to study protein interaction with other proteins, small molecules, metal ions, lipids, nucleic acids and carbohydrates; and nucleic acid interaction with small molecules. The drug discovery industry has utilized this approach to measure protein (or nucleic acid) interaction with drug candidates. ITC has been used to screen candidates, guide the design of potential drugs and validate the modelling used in structure-based drug design. Emerging disciplines including nanotechnology and drug delivery could benefit greatly from ITC in enhancing their understanding and control of nano-particle assembly, and drug binding and controlled release.

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“…Repeated published reports noted that copper may play a significant role in the conversion of PrP C to PrP Sc [6][7][8][9] (Fig. 2).…”

Section: Introductionmentioning

confidence: 61%

Using NMR spectroscopy to investigate the role played by copper in prion diseases

et al. 2020

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Prion diseases are a group of rare neurodegenerative disorders that develop as a result of the conformational conversion of normal prion protein (PrP C) to the disease-associated isoform (PrP Sc). The mechanism that actually causes disease remains unclear. However, the mechanism underlying the conformational transformation of prion protein is partially understood-in particular, there is strong evidence that copper ions play a significant functional role in prion proteins and in their conformational conversion. Various models of the interaction of copper ions with prion proteins have been proposed for the Cu (II)-binding, cell-surface glycoprotein known as prion protein (PrP). Changes in the concentration of copper ions in the brain have been associated with prion diseases and there is strong evidence that copper plays a significant functional role in the conformational conversion of PrP. Nevertheless, because copper ions have been shown to have both a positive and negative effect on prion disease onset, the role played by Cu (II) ions in these diseases remains a topic of debate. Because of the unique properties of paramagnetic Cu (II) ions in the magnetic field, their interactions with PrP can be tracked even at single atom resolution using nuclear magnetic resonance (NMR) spectroscopy. Various NMR approaches have been utilized to study the kinetic, thermodynamic, and structural properties of Cu (II)-PrP interactions. Here, we highlight the different models of copper interactions with PrP with particular focus on studies that use NMR spectroscopy to investigate the role played by copper ions in prion diseases.

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Influence of divalent copper, manganese and zinc ions on fibril nucleation and elongation of the amyloid-like yeast prion determinant Sup35p-NM

Cited by 12 publications

References 81 publications

Ion and seed dependent fibril assembly of a spidroin core domain

Ion and seed dependent fibril assembly of a spidroin core domain

Survey of the year 2009: applications of isothermal titration calorimetry

Using NMR spectroscopy to investigate the role played by copper in prion diseases

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