pH-dependence of the specific binding of Cu(II) and Zn(II) ions to the amyloid-β peptide

Ghalebani, Leila; Wahlström, Anna; Danielsson, Jens; Wärmländer, Sebastian K.T.S.; Gräslund, Astrid

doi:10.1016/j.bbrc.2012.04.043

Cited by 48 publications

(77 citation statements)

References 23 publications

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“…From ESI-MS analysis, Aβ(1-42) was confirmed to be entirely free of Met 35 oxidation or other PTMs, while solution NMR provided additional confidence that the final product obtained in a native unstructured state, and that chemical shifts were consistent with prior published work (Hou et al 2004;Long et al 2011;Nagata-Uchiyama et al 2007;Williamson et al 2006;Yan et al 2008;Danielsson et al 2006;Broersen et al 2011;Rezaei-Ghaleh et al 2011;Ghalebani et al 2012). In addition, the peptide was remarkably stable throughout NMR acquisition, easily providing for at least 1 week of spectral acquisition despite having near-physiological concentrations of salt present, which have been noted to reduce sample lives to <24 h (Williamson et al 2006).…”

Section: Discussionsupporting

confidence: 63%

“…Figure 4 displays a well-resolved HSQC spectrum of monomeric Aβ(1-42). Cross-peak positions are well-matched to previous spectra of either or Aβ(1-42) with similar buffer composition and temperature (Hou et al 2004;Long et al 2011;Nagata-Uchiyama et al 2007;Williamson et al 2006;Yan et al 2008;Danielsson et al 2006;Broersen et al 2011;Rezaei-Ghaleh et al 2011;Ghalebani et al 2012). In addition, samples maintained at 5 °C were stable for periods exceeding 1 week, which allowed confirmation of 1 H 15 N HSQC assignments through a longer triple-resonance 15 N-edited HNCACB experiment.…”

Section: Biophysical Characterization Of Aβ(1-42)mentioning

confidence: 96%

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A routine method for cloning, expressing and purifying Aβ(1–42) for structural NMR studies

2014

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Nuclear magnetic resonance (NMR) is a key technology in the biophysicist's toolbox for gaining atomic-level insight into structure and dynamics of biomolecules. Investigation of the amyloid-β peptide (Aβ) of Alzheimer's disease is one area where NMR has proven useful, and holds even more potential. A barrier to realizing this potential, however, is the expense of the isotopically enriched peptide required for most NMR work. Whereas most biomolecular NMR studies employ biosynthetic methods as a very cost-effective means to obtain isotopically enriched biomolecules, this approach has proven less than straightforward for Aβ. Furthermore, the notorious propensity of Aβ to aggregate during purification and handling reduces yields and increases the already relatively high costs of solid phase synthesis methods. Here we report our biosynthetic and purification developments that yield pure, uniformly enriched ¹⁵N and ¹³C¹⁵N Aβ(1-42), in excess of 10 mg/L of culture media. The final HPLC-purified product was stable for long periods, which we characterize by solution-state NMR, thioflavin T assays, circular dichroism, electrospray mass spectrometry, and dynamic light scattering. These developments should facilitate further investigations into Alzheimer's disease, and perhaps misfolding diseases in general.

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Section: Discussionsupporting

confidence: 63%

Section: Biophysical Characterization Of Aβ(1-42)mentioning

confidence: 96%

A routine method for cloning, expressing and purifying Aβ(1–42) for structural NMR studies

2014

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“…Oxidative stress and generation of reactive oxygen species (ROS) also play crucial roles in accelerating the peptide fibrillization which in turn can generate more ROS causing a deleterious vicious cycle of neurodegeneration [8, 9]. Earlier reports suggest that copper ions entrapped in A β fibrils are electrochemically active and can generate ROS depending on the microenvironment [10, 11]. Therefore, metal chelation by small antioxidant compounds like Curcumin and other phytochemicals could effectively contribute to the development of potential therapeutic strategies for protein misfolding diseases.…”

Section: Introductionmentioning

confidence: 99%

Inhibitory Effect of Curcumin-Cu(II) and Curcumin-Zn(II) Complexes on Amyloid-Beta Peptide Fibrillation

Banerjee

2014

Bioinorganic Chemistry and Applications

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Mononuclear complexes of Curcumin with Cu(II) and Zn(II) have been synthesized and, characterized and their effects on the fibrillization and aggregation of amyloid-beta (Aβ) peptide have been studied. FTIR spectroscopy and atomic force microscopy (AFM) observations demonstrate that the complexes can inhibit the transition from less structured oligomers to β-sheet rich protofibrils which act as seeding factors for further fibrillization. The metal complexes also impart more improved inhibitory effects than Curcumin on peptide fibrillization.

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“…In these regards, divalent metals can prevent the formation of active fibrillar structure at a specific stoichiometric ratio of 1:2 Aβ:metal ion [27], where the amounts of amorphous aggregates increases [28].…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Different zinc(II) complex species and binding modes at Aβ N-terminus drive distinct long range cross-talks in the Aβ monomers

Pietropaolo

Satriano

Strano

et al. 2015

Journal of Inorganic Biochemistry

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pH-dependence of the specific binding of Cu(II) and Zn(II) ions to the amyloid-β peptide

Cited by 48 publications

References 23 publications

A routine method for cloning, expressing and purifying Aβ(1–42) for structural NMR studies

A routine method for cloning, expressing and purifying Aβ(1–42) for structural NMR studies

Inhibitory Effect of Curcumin-Cu(II) and Curcumin-Zn(II) Complexes on Amyloid-Beta Peptide Fibrillation

Different zinc(II) complex species and binding modes at Aβ N-terminus drive distinct long range cross-talks in the Aβ monomers

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