Inhibitory Effect of Copper(II) on Zinc(II)-Induced Aggregation of Amyloid β-Peptide

Suzuki, Kenta; Miura, Tadao; Takeuchi, Hideo

doi:10.1006/bbrc.2001.5263

Cited by 85 publications

(83 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The idea arises from the finding that increased metal concentrations (mainly copper, iron and zinc) were present in the brains of Alzheimer's disease patients both in the amyloid plaques and in the cortical tissue [1][2][3]. Cu 2+ and Zn 2+ metals ions have a different physiological role and it has been observed that, in vitro, both promote (more zinc than copper) aggregation in amyloid fibrils and/or in amorphous aggregates [4][5][6][7][8][9][10][11]. Then, as a function of parameters like solvent's pH and metal concentration, these two ions have shown different behaviors; in particular, under physiological conditions, the amyloid peptide has a higher propensity to bind zinc, whereas, under mildly acidic conditions, as in physiological acidosis following an inflammatory process, copper is preferentially bound; in other words, zinc can protect against copper toxicity, which is induced by acidosis [12,13].…”

Section: Introductionmentioning

confidence: 99%

Thermal aggregation of β-lactoglobulin in presence of metal ions

Navarra

Leone

Militello

2007

Biophysical Chemistry

View full text Add to dashboard Cite

This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT AbstractIn this work, we report a study on the effects of zinc and copper ions on the heat-induced aggregation of β−Lactoglobulin (BLG). Kinetics investigations on aggregates growth by light scattering measurements and on secondary structure changes by FT-IR absorption measurementsshow the different role played by two metals during the whole process. In particular, the presence of zinc in solution promotes the formation of aggregates of BLG at a lower temperature than the copper. Then, fixed the temperature, formation of a large amount of aggregates, with a large dimension, is observed for the Zn-BLG in shorter time; on the contrary, the presence of the copper in solution does not affect the aggregation process but the secondary structure changes and the formation of different stronger intermolecular H-bonds, which probably lead to build a network of bonds that takes towards gelation. Our studies show as time evolution of aggregation process of BLG is dramatically affected by the presence of metal ions in solution and structural protein modifications are induced by different divalent metal ions.

show abstract

Section: Introductionmentioning

confidence: 99%

Thermal aggregation of β-lactoglobulin in presence of metal ions

Navarra

Leone

Militello

2007

Biophysical Chemistry

View full text Add to dashboard Cite

show abstract

“…Evidence shows that metal ions such as zinc, copper, and iron can be reduced with amyloid-β proteins and precipitated in the brain because amyloid βpeptide complexes possess a metalloprotein function by binding metal ions either with N-τ of the histidine imidazole ring and main chain amide nitrogens or N-Π atom [27,28,38,39]. Spectrophotometer experiments have established that the amyloid peptide reduces Fe(III) and Cu(II) to Fe(II) and Cu(I) when reducing reagents are available [29,30].…”

Section: Discussionmentioning

confidence: 99%

“…These short peptide sequences have motifs predicted to be structurally similar to portions of the 42 amino acid Aβ peptide, which is known to bind and reduce transition metals in the presence of a range of different biological reductants, including NADH [26][27][28][29][30]. Based on the PASTA algorithm, these sequences encode β-pairings known to participate in cross-β-fibrillar aggregates that are important for high-affinity metal binding [26,27,29,30].…”

Section: Chromate Reduction Is Encoded By Small Polypeptides Homologomentioning

confidence: 99%

A<i>β</i>-Like Peptide Displayed on Bacteriophage T7 Catalyzes Chromate and Uranyl Reduction

Jin¹,

Lin²,

Shang³

et al. 2013

JEP

View full text Add to dashboard Cite

In order to discover genes capable of catalyzing the reductive immobilization of toxic chromate and uranyl ions, we have created a T7 bacteriophage library containing cDNA from environmental microbes (i.e., Geobacter sulfurreducens and Shewanella oneidensis MR-1) that are known to mediate the reduction of chromate and uranyl ions. After three rounds of screening, ten bacteriophage mutants were found to mediate the NADH-dependent reduction of chromate and uranyl ions whose cDNA encodes polypeptide chains ranging 14 to 73 amino acids in length. All identified sequences contain disordered structural motifs similar to the β-amyloid peptide (Aβ) known to promote aggregation and formation of high-affinity metal binding sites. Confirmation of this structural similarity involved phage display of the 42 amino-acid Aβ-peptides that have been found to catalyze the NADH-dependent reduction of both chromate and uranyl ions. Transmission electron microscopy (TEM) and X-ray absorption near edge structure (XANES) measurements confirm that reduced uranium is present on the surface of bacteriophage expressing the Aβ-peptide. The surface-displayed Aβ-like peptide on bacteriophage has the potential to couple naturally occurring electron transfer shuttles present in soils to promote economically viable remediation of contaminated sites containing toxic chromate and uranyl ions.

show abstract

“…1(C) and (D)), as suggested by the appearance of a new Raman band component at ∼1554 cm −1 , besides to the ∼1565 cm −1 one due to free His (νC 4 =C 5 ), characteristic of the His − form bridging two metal ions through N π -and N τ -ligation (Fig. 2(A)) [10,15,18].…”

mentioning

confidence: 89%

“…In fact, Cu 2+ ion has been found to bind main-chain amide nitrogen in many protein or peptide-containing systems (i.e. soluble Cu(II)-amyloid β-peptide complex), since it is able to promote ionization of amide groups if a His residue is available as binding site [11,18].…”

mentioning

confidence: 99%

Chemical and physical characterization of thermal aggregation of model proteins modulated by zinc(II) and copper(II) ions

Torreggiani¹,

Navarra

Tinti

et al. 2016

BSI

View full text Add to dashboard Cite

Abstract. BACKGROUND:Metal ions are implicated in protein aggregation processes of several neurodegenerative pathologies, where the protein deposition occurs, and in the biotechnology field like the food technology where many processes in food manufacturing are based on thermal treatments. OBJECTIVE: The influence of Cu 2+ or Zn 2+ ions on the thermal aggregation process of Bovine β-lactoglobulin (BLG) and Bovine Serum Albumin (BSA), two protein models, was studied with the aim of delineating the role of these ions in the protein aggregation kinetics and to clarify the related molecular mechanisms. METHODS: The protein structure changes were monitored by Raman spectroscopy, whereas the aggregate growth was followed by Dynamic Light Scattering measurements. RESULTS: Both metal ions are able to favour the BLG aggregation, whereas only Zn 2+ ions have a promoter effect on the thermal aggregation of BSA. The reason of this different behaviour is that the BLG aggregation evolution is manly affected by the redistribution of charges, whereas that of BSA by the metal coordination binding which depends on metal. CONCLUSIONS: Raman spectroscopy, combined with dynamic light scattering experiments, was very useful in identifying the role played by Cu 2+ and Zn 2+ on the aggregation pathways of BLG and BSA. The results provide evidence for the role of histidine residues both in the redistribution of charges and in the two modes of metal binding that take place in BLG-and BSA-containing systems, respectively.

show abstract

Inhibitory Effect of Copper(II) on Zinc(II)-Induced Aggregation of Amyloid β-Peptide

Cited by 85 publications

References 35 publications

Thermal aggregation of β-lactoglobulin in presence of metal ions

Thermal aggregation of β-lactoglobulin in presence of metal ions

A<i>β</i>-Like Peptide Displayed on Bacteriophage T7 Catalyzes Chromate and Uranyl Reduction

Chemical and physical characterization of thermal aggregation of model proteins modulated by zinc(II) and copper(II) ions

Contact Info

Product

Resources

About

Inhibitory Effect of Copper(II) on Zinc(II)-Induced Aggregation of Amyloid β-Peptide

Cited by 85 publications

References 35 publications

Thermal aggregation of β-lactoglobulin in presence of metal ions

Thermal aggregation of β-lactoglobulin in presence of metal ions

A&lt;i&gt;β&lt;/i&gt;-Like Peptide Displayed on Bacteriophage T7 Catalyzes Chromate and Uranyl Reduction

Chemical and physical characterization of thermal aggregation of model proteins modulated by zinc(II) and copper(II) ions

Contact Info

Product

Resources

About

A<i>β</i>-Like Peptide Displayed on Bacteriophage T7 Catalyzes Chromate and Uranyl Reduction