Binding of iron(III) to the single tyrosine residue of amyloid β-peptide probed by Raman spectroscopy

Miura, Tadao; Suzuki, Kenta; Takeuchi, Hideo

doi:10.1016/s0022-2860(01)00807-9

Cited by 48 publications

(56 citation statements)

References 13 publications

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“…It has also been suggested that the peptide aggregates through intermolecular His-(N(tau))-Zn II -His(N(tau)) bridges. [24] The involvement of the three histidines as ligands has also been found by 1 H NMR measurements of Zn addition to Ab , which gave rise to broadening of the C2-H and C4-H resonances of His6, His13 and His14. [25] Recently, ESI-mass spectrometric analysis of Zn-Ab [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16] investigated by collision-induced dissociation confirmed the three histidines as ligands and proposed Arg5, but not Tyr10, as a fourth ligand.…”

Section: Introductionmentioning

confidence: 78%

“…[23] Raman spectroscopy studies on Zn-induced aggregates of Ab and Ab [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16] generated by addition of two-to fourfold excesses of Zn to the peptide have been reported. [24] The analysis suggested that all three histidines residues (6, 13 and 14) provide the primary metal binding sites and that Zn is bound to the N(tau) of His. The data also indicated that Tyr10 acted as a ligand at pH 7.4 (at least partially).…”

Section: Introductionmentioning

confidence: 99%

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Characterization of the Zn^II Binding to the Peptide Amyloid‐β^1–16 linked to Alzheimer's Disease

et al. 2005

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Aggregation of the human peptide amyloid-beta (Abeta) is a key event in Alzheimer's disease (AD). Zinc ions play an important role in AD and in Abeta aggregation. In vitro, Zn(II) binds to Abeta and accelerates its aggregation. In this work we have investigated Zn(II) binding to the synthetic peptide Abeta1-16, which contains the metal-binding domain of Abeta. Cd(II) was used to probe the Zn(II) site. Abeta1-16 bound one equivalent of Zn(II) with an apparent dissociation constant (Kd) of 10(-4) M. This Kd value is in the same range as the Zn concentration needed to precipitate Abeta. Circular dichroism and NMR indicated predominantly random-coil secondary structures of apo-Abeta1-16, Zn(II)-Abeta1-16 and Cd(II)-Abeta1-16, which were all highly dynamic and flexible. The three histidines at positions 6, 13 and 14 were suggested to be ligands to Zn(II) and Cd(II). Evidence that the aspartate at position 1 served as a fourth ligand to Zn(II) and Cd(II) was found at pH 8.7. 111Cd(II) NMR showed a resonance at 84 ppm, in line with a mixed oxygen-/nitrogen-ligand environment. The tyrosine at position 10 could be excluded as a ligand.

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Section: Introductionmentioning

confidence: 78%

Section: Introductionmentioning

confidence: 99%

Characterization of the Zn^II Binding to the Peptide Amyloid‐β^1–16 linked to Alzheimer's Disease

et al. 2005

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“…These three solvent-exchangeable NH signals further confirms the involvement of all three histidine residues in A␤ [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20] for metal binding, consistent with previous Raman spectroscopic studies (10), and is indicative of the absence of a bridging histidyl imidazole (in contrast to what has been previously suggested (10,13)), which would result in the loss of an imidazole NH signal. Tyr 10 was suggested to be a possible ligand for Cu 2ϩ and Fe 3ϩ binding (10,13,61), but was suggested not to be a ligand in other studies (55 fer transitions for a possible Tyr-Cu 2ϩ binding as described above. Our results also do not support the binding of the Nterminal amino group to the metal as previously suggested (50).…”

Section: Cumentioning

confidence: 93%

Catechol Oxidase-like Oxidation Chemistry of the 1–20 and 1–16 Fragments of Alzheimer's Disease-related β-Amyloid Peptide

Silva

Tay

2005

Journal of Biological Chemistry

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The Cu 2؉ complexes of the 1-16 and the 1-20 fragments of the Alzheimer's disease-related ␤-amyloid peptide (CuA␤) show significant oxidative activities toward a catechol-like substrate trihydroxylbenzene and plasmid DNA cleavage. The latter reflects possible oxidative stress to biological macromolecules, yielding supporting data to the pathological role of these soluble A␤ fragments. Abnormal metal-ion homeostasis has been closely associated with several neurodegenerative diseases, including Parkinson's, amyotrophic lateral sclerosis, Creutzfeldt-Jakob disease (i.e. human "mad cow" or prion disease), and Alzheimer's disease (AD) 1 (1-4). Because high cytoplasmic concentrations of free metal ions are toxic and potentially lethal, intricate physiological pathways have evolved to transport and distribute metal ions to their targets, which include enzymes and proteins (5). With aging, physiological processes responsible for accurate delivery of metal ions break down and "leakage" of free metal ions can cause toxic effects to cells (6, 7). Divalent ions of redox-active transition metals have often been associated with oxidative stress and closely involved in the chemistry of reactive oxygen species (ROS), including hydrogen peroxide as well as superoxide and hydroxyl radicals (8). Because increase in intracellular concentrations of metal ions is closely related to the effects of aging, oxidative stress, and AD, there is considerable interest in investigating the connection between malfunction of regulatory processes such as metal transport and the presence of ROS with the pathology of AD.The chemistry of redox-active metal complexes of ␤-amyloid peptide (A␤) has been an area of intense focus in the study of AD. The aggregation of A␤ within the neocortex is closely related to the pathology of AD and has been shown to be induced by metal binding (9, 10). The A␤ peptides are generated by the cleavage of the ubiquitous amyloid precursor protein by ␣, ␤, and ␥ secretases (11). A␤ in the form of insoluble plaques contains up to millimolar amounts of Zn 2ϩ , Cu 2ϩ , and Fe 3ϩ in the neocortical region of the brain (8); however, the cause/effect connection of the metallo-A␤ plaques with AD is still under debate (12). The metal coordination environment of the 1-40 and 1-42 peptides has been previously studied and their pH-dependent aggregation reported (10, 13). The results showed that the metal binding seemed to be non-stoichiometric with ϳ3.5 metal ions per pair of aggregated peptides and a cooperative binding pattern as the amount of aggregates increases (8). Because A␤ 1-42 and A␤ have been shown to bind Zn 2ϩ , Fe 3ϩ , and Cu 2ϩ with extremely low apparent dissociation constants by means of quantitative determination of the metal-complex precipitates (8), understanding of the metalbinding domain and its structure may shed light on the chemistry related to the neuropathology of AD.Although the coagulation of the peptide plaques leaves little doubt that interaction with cytoplasmic molecules is unlikely, smaller fragment...

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“…The tyrosine of human A␤ is thought to coordinate the metals that interact with the peptide (43,44), and we hypothesize that it may inappropriately coordinate with the metal active site of COX-2 (Fig. 5).…”

Section: Cox-2 Cross-links A␤mentioning

confidence: 99%

Peroxidase Activity of Cyclooxygenase-2 (COX-2) Cross-links β-Amyloid (Aβ) and Generates Aβ-COX-2 Hetero-oligomers That Are Increased in Alzheimer's Disease

Nagano

Huang

Moir

et al. 2004

Journal of Biological Chemistry

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Oxidative stress is associated with the neuropathology of Alzheimer's disease. We have previously shown that human A␤ has the ability to reduce Fe(III) and Cu(II) and produce hydrogen peroxide coupled with these metals, which is correlated with toxicity against primary neuronal cells. Cyclooxygenase (COX)-2 expression is linked to the progression and severity of pathology in AD. COX is a heme-containing enzyme that produces prostaglandins, and the enzyme also possesses peroxidase activity. Here we investigated the possibility of direct interaction between human A␤ and COX-2 being mediated by the peroxidase activity. Human A␤ formed dimers when it was reacted with COX-2 and hydrogen peroxide. Moreover, the peptide formed a cross-linked complex directly with COX-2. Such crosslinking was not observed with rat A␤, and the sole tyrosine residue specific for human A␤ might therefore be the site of cross-linking. Similar complexes of A␤ and COX-2 were detected in post-mortem brain samples in greater amounts in AD tissue than in age-matched controls. COX-2-mediated cross-linking may inhibit A␤ catabolism and possibly generate toxic intracellular forms of oligomeric A␤.

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Binding of iron(III) to the single tyrosine residue of amyloid β-peptide probed by Raman spectroscopy

Cited by 48 publications

References 13 publications

Characterization of the Zn^II Binding to the Peptide Amyloid‐β^1–16 linked to Alzheimer's Disease

Characterization of the Zn^II Binding to the Peptide Amyloid‐β^1–16 linked to Alzheimer's Disease

Catechol Oxidase-like Oxidation Chemistry of the 1–20 and 1–16 Fragments of Alzheimer's Disease-related β-Amyloid Peptide

Peroxidase Activity of Cyclooxygenase-2 (COX-2) Cross-links β-Amyloid (Aβ) and Generates Aβ-COX-2 Hetero-oligomers That Are Increased in Alzheimer's Disease

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Binding of iron(III) to the single tyrosine residue of amyloid β-peptide probed by Raman spectroscopy

Cited by 48 publications

References 13 publications

Characterization of the ZnII Binding to the Peptide Amyloid‐β1–16 linked to Alzheimer's Disease

Characterization of the ZnII Binding to the Peptide Amyloid‐β1–16 linked to Alzheimer's Disease

Catechol Oxidase-like Oxidation Chemistry of the 1–20 and 1–16 Fragments of Alzheimer's Disease-related β-Amyloid Peptide

Peroxidase Activity of Cyclooxygenase-2 (COX-2) Cross-links β-Amyloid (Aβ) and Generates Aβ-COX-2 Hetero-oligomers That Are Increased in Alzheimer's Disease

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Characterization of the Zn^II Binding to the Peptide Amyloid‐β^1–16 linked to Alzheimer's Disease

Characterization of the Zn^II Binding to the Peptide Amyloid‐β^1–16 linked to Alzheimer's Disease