Investigation of the affinity and selectivity of avian prion hexarepeat peptides for physiological divalent metal ions

Shields, S. Brookhart; Franklin, Sonya J.

doi:10.1016/j.jinorgbio.2007.01.004

Cited by 6 publications

(3 citation statements)

References 26 publications

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“…Up to four Cu 2+ ions are bound within the so called ''octarepeat region" (residues 60-91) [14][15][16][17][18][19][20][21][22][23][24], and two additional ions can be bound by His residues (His-96 and His-111) outside the tandem repeat region, in the so called ''amyloidogenic" region (residues 91-126) [25][26][27][28][29][30][31][32][33]. Prion or prion-like proteins of species different from mammals showed very similar copper binding to the N-terminal tandem repeat region [34][35][36][37][38][39][40][41][42][43][44].…”

Section: Introductionmentioning

confidence: 99%

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

Valensin

Gajda

Gralka

et al. 2010

Journal of Inorganic Biochemistry

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Section: Introductionmentioning

confidence: 99%

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

Valensin

Gajda

Gralka

et al. 2010

Journal of Inorganic Biochemistry

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“…32 Homologous Cu 2+ binding capability was identified for the tandem hexapeptide (PHNPGY) repeats located between residues 53 and 94, and here again the His residue plays a key role in the anchoring of Cu 2+ . 30,33,[44][45][46][47][48][49][50] Chicken prion repeat might bind copper in two different ways (i) an intra-repeat coordination mode, where Cu 2+ is bound to His imidazole and deprotonated amide nitrogen; (ii) an inter-repeat coordination mode, where only His imidazole nitrogens are bound to the metal ion. 47 Like in the human prion protein, two additional histidines at positions 110 and 124 are located outside the tandem repeat region in the chicken PrP sequence.…”

Section: Introductionmentioning

confidence: 99%

Copper(ii) coordination outside the tandem repeat region of an unstructured domain of chicken prion protein

Gralka

Valensin²,

Gajda³

et al. 2009

Mol. BioSyst.

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Combined potentiometric, calorimetric and spectroscopic methods were used to investigate the Cu(2+) binding ability and coordination behaviour of some peptide fragments related to the neurotoxic region of chicken Prion Protein. The systems studied were the following protein fragments: chPrP(106-114), chPrP(119-126), chPrP(108-127), chPrP(105-127) and chPrP(105-133).The complex formation always starts around pH 4 with the coordination of an imidazole nitrogen, followed by the deprotonation and binding of amide nitrogens from the peptidic backbone. At neutral pH, the {N(im), 3N(-)} binding mode is the preferred one. The amide nitrogens participating in the binding to the Cu(2+) ion derive from residues from the N-terminus side, with the formation of a six-membered chelate ring with the imidazolic side chain.Comparison of thermodynamic data for the two histydyl binding domains (around His-110 and His-124), clearly indicates that the closest to the hexarepeat domain (His-110) has the highest ability to bind Cu(2+) ions, although both of them have the same coordination mode. Conversely, in the case of the human neurotoxic peptide region, between the two binding sites, located at His-96 and His-111, the farthest from the tandem repeat region is the strongest one. Finally, thermodynamic data show that chicken peptide is a distinctly better ligand for coordination of copper ions with respect to the human fragment.

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“…The repeats consist of -PHNPGYsequences which anchor copper via His imidazoles. 10,[31][32][33][34][35][36][37][38] The amyloidogenic domain of chPrP shares several common features with hPrP91-127: 39,40 i. They both have two His residues spaced by almost the same number of amino acids.…”

Section: Introductionmentioning

confidence: 99%

The effect of a membrane-mimicking environment on the interactions of Cu²⁺with an amyloidogenic fragment of chicken prion protein

et al. 2017

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Prion proteins (PrP) from different species have the ability to tightly bind Cu ions. Copper coordination sites are located in the disordered and flexible N-terminal region which contains several His anchoring sites. Among them, two His residues are found in the so called amyloidogenic PrP region which is believed to play a key role in the process leading to oligomer and fibril formation. Both chicken and human amyloidogenic regions have a hydrophobic C-terminal region rich in Ala and Val amino acids. Recent findings revealed that this domain undergoes random coil to α-helix structuring upon interaction with membrane models. This interaction might strongly impact metal binding abilities either in terms of donor sets or affinity. In this study we investigated Cu interaction with an amyloidogenic fragment, chPrP105-140, derived from chicken prion protein (chPrP), in different solution environments. The behavior of the peptide and its metal complexes was analyzed in water and in the presence of negative and positive charged membrane mimicking environments formed by sodium dodecyl sulfate (SDS) and dodecyl trimethyl ammonium chloride (DTAC) micelles. The metal coordination sphere, the metal binding affinity and stoichiometry were evaluated by combining spectroscopic and potentiometric methods. Finally we compare copper(ii) interactions with human and chicken amyloidogenic fragments. Our results indicate that the chicken amyloidogenic fragment is a stronger copper ligand than the human amyloidogenic fragment.

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Investigation of the affinity and selectivity of avian prion hexarepeat peptides for physiological divalent metal ions

Cited by 6 publications

References 26 publications

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

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

Copper(ii) coordination outside the tandem repeat region of an unstructured domain of chicken prion protein

The effect of a membrane-mimicking environment on the interactions of Cu²⁺with an amyloidogenic fragment of chicken prion protein

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Investigation of the affinity and selectivity of avian prion hexarepeat peptides for physiological divalent metal ions

Cited by 6 publications

References 26 publications

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

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

Copper(ii) coordination outside the tandem repeat region of an unstructured domain of chicken prion protein

The effect of a membrane-mimicking environment on the interactions of Cu2+with an amyloidogenic fragment of chicken prion protein

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The effect of a membrane-mimicking environment on the interactions of Cu²⁺with an amyloidogenic fragment of chicken prion protein