Interactions of Cu<sup>2+</sup>ions with chicken prion tandem repeats

Stańczak, Paweł; Łuczkowski, Marek; Juszczyk, Paulina; Grzonka, Zbigniew; Kozłowski, Henryk

doi:10.1039/b405753h

Cited by 50 publications

(62 citation statements)

References 20 publications

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“…Comparison of the binding abilities between demegens and hexapeptides from chicken prion proteins allowed also to make some suggestions (Fig. 18C-E) [42]. Trimeric peptide (3-Hex) at low pH range exhibits the multi-imidazolic coordination mode and forms more stable complexes with Cu 2+ ion than Ac-DMG-NH 2 .…”

Section: Coordination Properties Of Demegen P-113 Towards Cu 2+ Ionsmentioning

confidence: 99%

“…The coordination pattern of chicken hexapeptide depends strongly on the number of hexapeptide units. Single hexapeptide unit binds copper ion in the physiological pH by {N im , N − } donor sets in the main trans/trans amide bond isomer [42][43][44]. The involvement of the consecutive amide nitrogen atoms in metal ion chelatation is disrupted by the presence of Pro residue between Asn and Gly residues.…”

Section: Chicken Prion Proteinmentioning

confidence: 99%

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Specificity in the Cu2+ interactions with prion protein fragments and related His-rich peptides from mammals to fishes

Kozłowski

Janicka-Kłos²,

Stańczak³

et al. 2008

Coordination Chemistry Reviews

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Section: Coordination Properties Of Demegen P-113 Towards Cu 2+ Ionsmentioning

confidence: 99%

Section: Chicken Prion Proteinmentioning

confidence: 99%

Specificity in the Cu2+ interactions with prion protein fragments and related His-rich peptides from mammals to fishes

Kozłowski

Janicka-Kłos²,

Stańczak³

et al. 2008

Coordination Chemistry Reviews

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“…Increasing the copper amount, the copper(II) is bound to each octa-repeat by means of one imidazole nitrogen, two amide nitrogens from the two glycine residues and one carbonyl oxygen [128][129][130]. Although it has been reported that the tetrahexarepeat peptide can bind up to four copper atoms, being in this similar to human PrP C even if with a lower affinity [133], other results questioned this finding [87,132,137]. UV-vis and CD studies carried out on chicken hexameric peptide fragments containing two histidine residues indicate that this peptide binds only one copper(II), evidencing the significant role of Gly residues in copper coordination for the mammalian octameric region [132].…”

Section: Prion and Copper(ii) Coordination Features: Mammal Vs Avianmentioning

confidence: 99%

“…Copper complex species with chPrP C peptide fragments show binding constant values [84,87,[133][134][135]140] lower than those found in SOD-1 enzymes. This appears in contrast with the biological significance of a true SOD-like enzyme in vivo, which has to bind strongly the metal ion.…”

mentioning

confidence: 99%

Prion Proteins Leading to Neurodegeneration

Mendola

Pietropaolo²,

Pappalardo³

et al. 2008

CAR

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Prion diseases are fatal neurodegenerative disorders related to the conformational alteration of the prion protein (PrP C ) into a pathogenic and protease-resistant isoform PrP Sc . PrP C is a cell surface glycoprotein expressed mainly in the central nervous system and despite numerous efforts to elucidate its physiological role, the exact biological function remains unknown. Many lines of evidences indicate that prion is a copper binding protein and thus involved in the copper metabolism. Prion protein is not expressed only in mammals but also in other species such as birds, reptiles and fishes. However, it is noteworthy to point out that prion diseases are only observed in mammals while they seem to be spared to other species. The chicken prion protein (chPrP C ) shares about 30% of identity in its primary sequence with mammal PrP C . Both types of proteins have an N-terminal domain endowed with tandem amino acid repeats (PHNPGY in the avian protein, PHGGGWQ in mammals), followed by a highly conserved hydrophobic core. Furthermore, NMR studies have highlighted a similar globular domain containing three α-helices, one short 3 10 -helix and a short antiparallel β-sheet. Despite this structural similarity, it should be noted that the normal isoform of mammalian PrP C is totally degraded by proteinase K, while avian PrP C is not, thereby producing N-terminal domain peptide fragments stable to further proteolysis. Notably, the hexarepeat domain is considered essential for protein endocytosis, and it is supposed to be the analogous copper-binding octarepeat region of mammalian prion proteins. The number of copper binding sites, the affinity and the coordination environment of metal ions are still matter of discussion for both mammal and avian proteins.In this review, we summarize the similarities and the differences between mammalian and avian prion proteins, as revealed by studies carried out on the entire protein and related peptide fragments, using a range of experimental and computational approaches. In addition, we report the metaldriven conformational alteration, copper binding modes and the superoxide dismutase-like (SODlike) activity of the related copper(II) complexes. necessary to obtain data on copper ions binding, complex species, affinity and coordination mode, in order to have valuable grounding to explain the so-called "metal paradox".As shown in the previous example of rat and human Aβ, a useful approach consists in making comparative studies on proteins and peptides of different organisms. This approach allows us also to obtain information on the possible biological role of the proteins. Currently another common aspect of several proteins or peptides involved in such diseases is that their biological function remains unknown.8 PrP C is a highly conserved protein in mammals, but genes encoding homologous prion proteins have been reported in different species such as avians/birds, turtles, amphibians and fish [53][54][55][56][57][58][59]. It is important to point out that prion diseases are ob...

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“…The molar ratio 1:1 was not studied due to the tendency of lanthanide ions to achieve high coordination numbers, and inadequate number of donor atoms of the ligand. Determined pK w for dimethyl sulfoxide/ water (30:70) was 14.501 [31]. The protonation constants of the N,N'-bis(5-methylsalicylidene)-4-methyl-1,3-phenylenediamine, the selection of the models as well as the stability constants of the complexes were determined with HYPER-QUAD software which uses the nonlinear method of least squares [32].…”

Section: Introductionmentioning

confidence: 99%

Potentiometric determination of novel complexes of selected lanthanide ions with N,N’-bis(5-methylsalicylidene)-4-methyl-1,3-phenylenediamine

2017

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The stability constants of the complexes formed in the N,N '-bis(5-methylsalicylidene)-4-methyl-1,3-phenylenediamine (H 2 L) and La(III), Eu(III), Gd(III), Ho(III), and Lu(III) ion systems were determined in solution with the potentiometric method. The pH-metric titrations were performed in dimethyl sulfoxide/water (v:v, 30:70) mixture at 25.0 °C in 0.1 M LiNO 3 ionic strength. The tests were performed for systems with Ln(III) to H 2 L 1:2 and 1:3 molar ratio but only data of the systems with the metal/ligand ratio 1:2 were taken into calculation. The molar ratio 1:1 was not studied because of the high coordination numbers of the lanthanide ions, and inadequate donor atoms of the ligand. Computer analysis (HYPERQUAD software) of potentiometric data indicated that in solution the lanthanide (Ln) complexes exist as LnL 2 , Ln(HL) 2 , and Ln(H 2 L) 2 forms, depending on pH unlike to the solid state where only one form of Ln(H 2 L) 2 occurs. Formation constants increase with decreasing size of the Ln(III) ions. Moreover, complex formation in the Ln 3+ /H 2 L systems in solution was performed using UV-Vis spectrophotometric titration.

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Interactions of Cu²⁺ions with chicken prion tandem repeats

Cited by 50 publications

References 20 publications

Specificity in the Cu2+ interactions with prion protein fragments and related His-rich peptides from mammals to fishes

Specificity in the Cu2+ interactions with prion protein fragments and related His-rich peptides from mammals to fishes

Prion Proteins Leading to Neurodegeneration

Potentiometric determination of novel complexes of selected lanthanide ions with N,N’-bis(5-methylsalicylidene)-4-methyl-1,3-phenylenediamine

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Interactions of Cu2+ions with chicken prion tandem repeats

Cited by 50 publications

References 20 publications

Specificity in the Cu2+ interactions with prion protein fragments and related His-rich peptides from mammals to fishes

Specificity in the Cu2+ interactions with prion protein fragments and related His-rich peptides from mammals to fishes

Prion Proteins Leading to Neurodegeneration

Potentiometric determination of novel complexes of selected lanthanide ions with N,N’-bis(5-methylsalicylidene)-4-methyl-1,3-phenylenediamine

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Interactions of Cu²⁺ions with chicken prion tandem repeats