Copper(II) Coordination to Amyloid β: Murine versus Human Peptide

Eury, Hélène; Bijani, Christian; Faller, Peter; Hureau, Christelle

doi:10.1002/anie.201005838

Cited by 78 publications

(113 citation statements)

References 36 publications

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“…Our observations agree with the pK a values of 7.7 and 6.2 reported for the hAb and mAb. [21] The activation energies of the coordination switching were determined to be 65(3) kJ mol À1 for hAb 16 -Cu, and 73(2) kJ mol À1 for mAb 16 -Cu (Figure 3 d). These sizeable values may be due to the difficulty in deprotonating the amide bond (Scheme 1 and Supporting Information).…”

Section: Introduction Of a Fluorescent Probe To Amyloid-b To Reveal Kmentioning

confidence: 98%

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Introduction of a Fluorescent Probe to Amyloid‐β to Reveal Kinetic Insights into Its Interactions with Copper(II)

et al. 2014

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The kinetics of the interactions between amyloid‐β (Aβ) and metal ions are crucial to understanding the physiological and pathological roles of Aβ in the normal brain and in Alzheimer’s disease. Using the quenching of a fluorescent probe by Cu2+, the mechanism of Aβ/Cu2+ interactions in physiologically relevant conditions has been elucidated. Cu2+ binds to Aβ at a near diffusion‐limited rate, initially forming component I. The switching between component I and II occurs on the second timescale, with a significant energy barrier. Component I is much more reactive towards Cu2+ ligands and likely responsible for initial Aβ dimer formation. Clioquinol (CQ) is shown to sequester Cu2+ more effectively than other tested ligands. These findings have implications for the potential roles of Aβ in regulating neurotransmission, and for the screening of small molecules targeting Aβ–metal interactions.

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Section: Introduction Of a Fluorescent Probe To Amyloid-b To Reveal Kmentioning

confidence: 98%

“…[20,21] The association timescales (ca. 0.2 ms) in the presence of the physiological 10 mm Cu 2+ and the dissociation (ca.…”

Section: Introduction Of a Fluorescent Probe To Amyloid-b To Reveal Kmentioning

confidence: 99%

Introduction of a Fluorescent Probe to Amyloid‐β to Reveal Kinetic Insights into Its Interactions with Copper(II)

et al. 2014

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“…Metals are known to play a key role in this oxidative stress and also to be associated with peptide aggregation, at the core of the pathology (Faller et al, 2013;Viles, 2012). More specifically, Cu II has been found to form a complex with the amyloid peptide for which aggregation is one of the major hallmarks of AD (Eury et al, 2011;Faller et al, 2014). This has triggered significant ongoing interest in the development of chelators able to interact with metals in the context of AD (Santos et al, 2016;Conte-Daban et al, 2017).…”

Section: Chemical Contextmentioning

confidence: 99%

Crystal structure of catena-poly[[[dichloridocopper(II)]-{μ-tert-butyl N-methyl-N-[4-(6-{[4-(pyridin-2-yl-κN)-1H-1,2,3-triazol-1-yl-κN ³]methyl}-1,3-benzothiazol-2-yl)phenyl]carbamato}] acetonitrile monosolvate]

Pocinho¹,

Duhayon²,

Gras³

et al. 2018

Acta Cryst E

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In the title coordination polymer, {[CuCl2(C27H26N6O2S)]·CH3CN} n , the copper(II) ion is fivefold coordinated, with an almost perfect square-pyramidal coordination sphere. In the equatorial plane, it is ligated to a pyridine N atom and an N atom of the triazole unit and to two Cl− ions, while the apical position is occupied by the carbonyl O atom of the tert-butyl carbamate group. In the crystal, the polymer chains propagate in the [11-1] direction, with the acetonitrile solvent molecules linked to the chain by C—H...N hydrogen bonds. The chains are linked by C—H...Cl hydrogen bonds forming sheets parallel to the plane (011). The crystal packing is further consolidated by C—H...π interactions and offset π–π stacking interactions [intercentroid distance = 3.6805 (15) Å], forming a three-dimensional supramolecular structure.

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“…The binding geometries and coordination spheres are also pH dependent when aC u 2 + ion binds to mAb.E ury et al [9] pointedo ut two coordination spheres in different pH ranges for Cu 2 + -mAb [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16] complex, that is, the 2N2O component I m [NH 2 (Asp1), CO, COO À (Asp/Glu), N imi (His6/14)] at pH < 6.2, and 3N1O coordination component II m ,[ NH 2 (Asp1), CO (Asp1-Ala2), N( Gly5-His6), N imi (His6)] at pH > 6.2 (where N imi is an itrogen atom of an imidazole side group). The latter is consistent with the component proposed by Hong et al at pH 7.4.…”

Section: Introductionmentioning

confidence: 97%

“…At physiological pH, two Cu 2 + binding modes, termedc omponents Ia nd II, coexist and are generally accepted. Both componentsIand II are 3N1O modes, specifically, I [NH 2 (Asp1), CO (Asp1-Ala2), His6, His13/14] at pH < 7.7 [9] (or 7.8 [10] ), andI I[ NH 2 (Asp1), N(Asp1-Ala2), CO (Ala2-Glu3),H is6/ 13/14]a tp H> 7.7 [9] (or 7.8 [10] ). It is cleart hat the transition between Ia nd II is pH-driven with pH 7.8 as an approximate threshold.…”

Section: Introductionmentioning

confidence: 99%

Molecular Simulations of Human and Mouse Aβ_1–16 at Different pH Values: Structural Characteristics toward Understanding Cu²⁺‐Coordinated Amyloid Beta Spheres

Zhang

Zhu

et al. 2016

ChemPhysChem

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As the main sequence responsible for metal ion coordination in the amyloid beta (Aβ) peptide, Aβ1-16 plays a key role in the understanding of the aggregation of Aβ induced by Cu(2+) ions. There is no consensus on the nature of the coordination sphere of the Cu(2+) -Aβ complex so far due to the amorphous conformation of the Aβ1-16 peptide itself and the pH dependence of Cu(2+) -Aβ coordination. The simulation reported here reveals that human Aβ1-16 monomer has a U-shape morphology, which is preserved at any pH. This morphology accommodates Cu(2+) ions with several binding sites and is also the basis for establishing a center-distance statistical method (CDSM). Based on this CDSM, specific histidine residues for a Cu(2+) -coordinated sphere are identified and the corresponding accurate pH range is established, indicating that the CDSM can be used as a reference to predict the potential coordination sites of metal ions in other amorphous peptides. By contrast, mouse Aβ1-16 monomer has a more open and random morphology than human Aβ1-16 due to the differences of three sequence positions. These mutations not only reduce the number of binding sites required by a stable Cu(2+) -binding sphere but also diminish the capacity to generate salt bridges compared to the human peptide. These observations offer insights into the roles of three residues that differ in the mouse Aβ1-16 and perhaps into the reasons mice seldom develop Alzheimer's disease.

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Copper(II) Coordination to Amyloid β: Murine versus Human Peptide

Cited by 78 publications

References 36 publications

Introduction of a Fluorescent Probe to Amyloid‐β to Reveal Kinetic Insights into Its Interactions with Copper(II)

Introduction of a Fluorescent Probe to Amyloid‐β to Reveal Kinetic Insights into Its Interactions with Copper(II)

Crystal structure of catena-poly[[[dichloridocopper(II)]-{μ-tert-butyl N-methyl-N-[4-(6-{[4-(pyridin-2-yl-κN)-1H-1,2,3-triazol-1-yl-κN ³]methyl}-1,3-benzothiazol-2-yl)phenyl]carbamato}] acetonitrile monosolvate]

Molecular Simulations of Human and Mouse Aβ_1–16 at Different pH Values: Structural Characteristics toward Understanding Cu²⁺‐Coordinated Amyloid Beta Spheres

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Copper(II) Coordination to Amyloid β: Murine versus Human Peptide

Cited by 78 publications

References 36 publications

Introduction of a Fluorescent Probe to Amyloid‐β to Reveal Kinetic Insights into Its Interactions with Copper(II)

Introduction of a Fluorescent Probe to Amyloid‐β to Reveal Kinetic Insights into Its Interactions with Copper(II)

Crystal structure of catena-poly[[[dichloridocopper(II)]-{μ-tert-butyl N-methyl-N-[4-(6-{[4-(pyridin-2-yl-κN)-1H-1,2,3-triazol-1-yl-κN 3]methyl}-1,3-benzothiazol-2-yl)phenyl]carbamato}] acetonitrile monosolvate]

Molecular Simulations of Human and Mouse Aβ1–16 at Different pH Values: Structural Characteristics toward Understanding Cu2+‐Coordinated Amyloid Beta Spheres

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Crystal structure of catena-poly[[[dichloridocopper(II)]-{μ-tert-butyl N-methyl-N-[4-(6-{[4-(pyridin-2-yl-κN)-1H-1,2,3-triazol-1-yl-κN ³]methyl}-1,3-benzothiazol-2-yl)phenyl]carbamato}] acetonitrile monosolvate]

Molecular Simulations of Human and Mouse Aβ_1–16 at Different pH Values: Structural Characteristics toward Understanding Cu²⁺‐Coordinated Amyloid Beta Spheres