Copper binding to chicken and human prion protein amylodogenic regions: Differences and similarities revealed by Ni2+ as a diamagnetic probe

Valensin, Daniela; Gajda, Karolina; Gralka, Ewa; Valensin, Gianni; Kamysz, Wojciech; Kozłowski, Henryk

doi:10.1016/j.jinorgbio.2009.10.008

Cited by 29 publications

(20 citation statements)

References 58 publications

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“…These data reveal a significant difference in the nickel(II) and copper(II) binding sites of the peptides: His96 was found to predominate almost completely for nickel(II) ions, while the opposite order, but with comparable concentrations, was reported for copper(II) [25,26]. The results on the copper(II) and nickel(II) complexes of the peptide fragment of chicken prion protein, ChPrP (108-127), were reported very recently [46]. This peptide contains also two histidines (His110 and His124) and corresponds to the 91-115 region of human prion protein.…”

Section: Discussionmentioning

confidence: 85%

Nickel(II) complexes of the multihistidine peptide fragments of human prion protein

Turi

Kállay

Szikszai

et al. 2010

Journal of Inorganic Biochemistry

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Section: Discussionmentioning

confidence: 85%

Nickel(II) complexes of the multihistidine peptide fragments of human prion protein

Turi

Kállay

Szikszai

et al. 2010

Journal of Inorganic Biochemistry

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“…PrP106-126 has a high tendency to aggregate into b-sheet structures, forms amyloid fibrils in vitro, and becomes partially resistant to proteolysis. [23][24][25][26][27][28][29] Studies on prion inhibitors have been reported. 19,20 Another study has shown that early ordered oligomers are stacked by an interface of hydrophobic C-terminal residues (A113-G126), which may increase the fibril growth rate and form the fibril structure.…”

Section: Introductionmentioning

confidence: 99%

“…17,18 Recent studies have reported that oligomerization of PrP106-126 is caused by association of ordered b-hairpin monomers rather than disordered monomers. 23,24,27,28,30 Some researchers have reported the inhibitory effects of small molecules on either the aggregation behavior or neurotoxicity of PrP106-126. 21 The spanning fragment of Asn108-Met109-Lys110-His111-Met112 in PrP106-126 exhibits a ''turn-like'' conformation, wherein His111 is located before the starting point of an a-helix; the effects of His111 are important in modulating the conformational flexibility and heterogeneity of PrP106-126.…”

Section: Introductionmentioning

confidence: 99%

Influence of gold–bipyridyl derivants on aggregation and disaggregation of the prion neuropeptide PrP106–126

Zhao

Wang

et al. 2014

Metallomics

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Metal complexes can effectively inhibit the aggregation of amyloid peptides, such as Aβ, human islet amyloid polypeptide, and prion neuropeptide PrP106-126. Gold (Au) complexes exhibited better inhibition against PrP106-126 aggregation, particularly the Au-bipyridyl (bpy) complex; however, the role of different ligand configurations remains unclear. In the present study, three derivants of Au-bpy complexes, namely, [Au(Me2bpy)Cl2]Cl, [Au(t-Bu2bpy)Cl2]Cl, and [Au(Ph2bpy)Cl2]Cl, were investigated to determine their influence on the aggregation and disaggregation of PrP106-126. The steric and aromatic effects of the ligand resulted in enhanced binding affinity. Inhibition was significantly affected by a large ligand. The neurotoxicity of the SH-SY5Y cells induced by PrP106-126 was reduced by the three Au-bpy derivants. However, the disaggregation ability was not in accordance with the results obtained for selected complexes during inhibition, suggesting a different mechanism of interaction between gold complexes and PrP106-126. The key peptide residues contributed to both the inhibition and disaggregation capabilities through the metal coordination and the hydrophobic interaction with the metal complexes. Thus, understanding the aggregation mechanism of the prion peptide would be helpful in designing novel metal-based drugs against amyloid fibril formation.

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“…- Valensin et al (2010) reported that HuPrP possesses two copper binding sites localized at His-96 and His-111 in the so called "amylodogenic" or neurotoxic region (residues 91-126) and chicken PrP possesses a similar region (PrP(105-140)) containing two His (His-110 and His-124) and an identical hydrophobic tail of 15 amino acids rich in Ala and Gly [Valensin et al (2010)]. • 2009:…”

Section: A Detailed Review On Prp Hydrophobic Regionmentioning

confidence: 99%

A Survey and a Molecular Dynamics Study on the (Central) Hydrophobic Region of Prion Proteins

Zhang¹,

Wang

2014

CPB

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Prion diseases are invariably fatal neurodegenerative diseases that affect humans and animals. Unlike most other amyloid forming neurodegenerative diseases, these can be highly infectious. Prion diseases occur in a variety of species. They include the fatal human neurodegenerative diseases Creutzfeldt-Jakob Disease (CJD), Fatal Familial Insomnia (FFI), Gerstmann-Strussler-Scheinker syndrome (GSS), Kuru, the bovine spongiform encephalopathy (BSE or 'mad-cow' disease) in cattle, the chronic wasting disease (CWD) in deer and elk, and scrapie in sheep and goats, etc. Transmission across the species barrier to humans, especially in the case of BSE in Europe, CWD in North America, and variant CJDs (vCJDs) in young people of UK, is a major public health concern. Fortunately, scientists reported that the hydrophobic region of prion proteins (PrP) controls the formation of diseased prions. This article gives a detailed survey on PrP hydrophobic region and does molecular dynamics studies of human to confirm some findings from the survey.

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Copper binding to chicken and human prion protein amylodogenic regions: Differences and similarities revealed by Ni2+ as a diamagnetic probe

Cited by 29 publications

References 58 publications

Nickel(II) complexes of the multihistidine peptide fragments of human prion protein

Nickel(II) complexes of the multihistidine peptide fragments of human prion protein

Influence of gold–bipyridyl derivants on aggregation and disaggregation of the prion neuropeptide PrP106–126

A Survey and a Molecular Dynamics Study on the (Central) Hydrophobic Region of Prion Proteins

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