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Studies on the interactions of copper and zinc ions with β-amyloid peptides by a surface plasmon resonance biosensor.

Yao F, Zhang R, Tian H, Li X - Int J Mol Sci (2012)

Bottom Line: Our observations indicate that the immobilized Aβ undergoes a conformational change upon exposure to the metal ions.A difference in metal binding affinity between Aβ(1-28) and Aβ(1-42) was also detected.The results suggest that SPR is an effective method to characterize the interactions between Aβ and metal ions.

View Article: PubMed Central - PubMed

Affiliation: College of Chemistry and Chemical Engineering, Graduate University, Chinese Academy of Sciences, Beijing, 100049, China; E-Mail: yaofuj09b@mails.gucas.ac.cn.

ABSTRACT
The aggregation of β-amyloid peptide (Aβ) into fibrils plays an important role in the pathogenesis of Alzheimer's disease (AD). Metal ions including copper and zinc are closely connected to the precipitation and toxicity of Aβ. In this study, a surface plasmon resonance (SPR) biosensor was constructed to investigate the interactions between Aβ and metal ions. Aβ peptide was immobilized on the SPR chip surface through a preformed alkanethiol self-assembled monolayer (SAM). Our observations indicate that the immobilized Aβ undergoes a conformational change upon exposure to the metal ions. A difference in metal binding affinity between Aβ(1-28) and Aβ(1-42) was also detected. The results suggest that SPR is an effective method to characterize the interactions between Aβ and metal ions.

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Related in: MedlinePlus

The sensorgrams for the interactions between Zn2+ ions and the Aβ1–28 peptides. Various concentrations (50, 100, 200, 300, 600, 700 and 800 μM, from top to bottom) of Zn2+ ions were injected onto the Aβ1–28 sensorchip. Arrows indicate Zn2+ ions starting to flow onto immobilized Aβ1–28 and when the flowing of metal ions ends, respectively.
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Related In: Results  -  Collection

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f2-ijms-13-11832: The sensorgrams for the interactions between Zn2+ ions and the Aβ1–28 peptides. Various concentrations (50, 100, 200, 300, 600, 700 and 800 μM, from top to bottom) of Zn2+ ions were injected onto the Aβ1–28 sensorchip. Arrows indicate Zn2+ ions starting to flow onto immobilized Aβ1–28 and when the flowing of metal ions ends, respectively.

Mentions: Figure 2 shows the sensorgrams of various Zn2+ concentrations flowing over the Aβ1–28 sensor chip. In these experiments, EDTA (10 mM) was used to regenerate the surface. Therefore, a single chip can be used repeatedly for multiple samples. As shown in Figure 2, increasing Zn2+ concentrations results in a greater SPR dip shift. When 600 μM Zn2+ flowed over the Aβ1–28-covered SPR sensor, the metal ions caused a net change of 0.0075°, which can be attributed to the binding of Zn2+ ions to Aβ1–28 resulting in conformational changes of the peptide molecules.


Studies on the interactions of copper and zinc ions with β-amyloid peptides by a surface plasmon resonance biosensor.

Yao F, Zhang R, Tian H, Li X - Int J Mol Sci (2012)

The sensorgrams for the interactions between Zn2+ ions and the Aβ1–28 peptides. Various concentrations (50, 100, 200, 300, 600, 700 and 800 μM, from top to bottom) of Zn2+ ions were injected onto the Aβ1–28 sensorchip. Arrows indicate Zn2+ ions starting to flow onto immobilized Aβ1–28 and when the flowing of metal ions ends, respectively.
© Copyright Policy - open-access
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC3472777&req=5

f2-ijms-13-11832: The sensorgrams for the interactions between Zn2+ ions and the Aβ1–28 peptides. Various concentrations (50, 100, 200, 300, 600, 700 and 800 μM, from top to bottom) of Zn2+ ions were injected onto the Aβ1–28 sensorchip. Arrows indicate Zn2+ ions starting to flow onto immobilized Aβ1–28 and when the flowing of metal ions ends, respectively.
Mentions: Figure 2 shows the sensorgrams of various Zn2+ concentrations flowing over the Aβ1–28 sensor chip. In these experiments, EDTA (10 mM) was used to regenerate the surface. Therefore, a single chip can be used repeatedly for multiple samples. As shown in Figure 2, increasing Zn2+ concentrations results in a greater SPR dip shift. When 600 μM Zn2+ flowed over the Aβ1–28-covered SPR sensor, the metal ions caused a net change of 0.0075°, which can be attributed to the binding of Zn2+ ions to Aβ1–28 resulting in conformational changes of the peptide molecules.

Bottom Line: Our observations indicate that the immobilized Aβ undergoes a conformational change upon exposure to the metal ions.A difference in metal binding affinity between Aβ(1-28) and Aβ(1-42) was also detected.The results suggest that SPR is an effective method to characterize the interactions between Aβ and metal ions.

View Article: PubMed Central - PubMed

Affiliation: College of Chemistry and Chemical Engineering, Graduate University, Chinese Academy of Sciences, Beijing, 100049, China; E-Mail: yaofuj09b@mails.gucas.ac.cn.

ABSTRACT
The aggregation of β-amyloid peptide (Aβ) into fibrils plays an important role in the pathogenesis of Alzheimer's disease (AD). Metal ions including copper and zinc are closely connected to the precipitation and toxicity of Aβ. In this study, a surface plasmon resonance (SPR) biosensor was constructed to investigate the interactions between Aβ and metal ions. Aβ peptide was immobilized on the SPR chip surface through a preformed alkanethiol self-assembled monolayer (SAM). Our observations indicate that the immobilized Aβ undergoes a conformational change upon exposure to the metal ions. A difference in metal binding affinity between Aβ(1-28) and Aβ(1-42) was also detected. The results suggest that SPR is an effective method to characterize the interactions between Aβ and metal ions.

Show MeSH
Related in: MedlinePlus