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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 sensorgram for the interactions between Cu2+ ions and Aβ1–42. Various concentrations (50, 100, 200, 300, and 400 μM, from top to bottom) of Cu2+ ions were injected onto the Aβ1–42 sensorchip. The inset shows the calibration curve for the interactions between various concentrations of Cu2+ with Aβ1–42. Each value represents the mean ± standard deviation of three separate injections. Arrows indicate Cu2+ ions starting to flow onto immobilized Aβ1–28 and when the flow of metal ions ends, respectively.
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f6-ijms-13-11832: The sensorgram for the interactions between Cu2+ ions and Aβ1–42. Various concentrations (50, 100, 200, 300, and 400 μM, from top to bottom) of Cu2+ ions were injected onto the Aβ1–42 sensorchip. The inset shows the calibration curve for the interactions between various concentrations of Cu2+ with Aβ1–42. Each value represents the mean ± standard deviation of three separate injections. Arrows indicate Cu2+ ions starting to flow onto immobilized Aβ1–28 and when the flow of metal ions ends, respectively.

Mentions: Similar results were obtained for the Cu-Aβ1–42 interaction. As shown in Figure 6, the SPR angle shift increased with an increase of Cu2+ bound to the Aβ1–42-immobilized sensor chip. The calibration curve generated from the sensor exposed to different concentrations of Cu2+ is shown in the Figure 6 inset. A strong correlation coefficient (R2 = 0.99) was obtained for the linear regression equation calculated using Cu2+ concentrations ranging from 50 to 400 μM.


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 sensorgram for the interactions between Cu2+ ions and Aβ1–42. Various concentrations (50, 100, 200, 300, and 400 μM, from top to bottom) of Cu2+ ions were injected onto the Aβ1–42 sensorchip. The inset shows the calibration curve for the interactions between various concentrations of Cu2+ with Aβ1–42. Each value represents the mean ± standard deviation of three separate injections. Arrows indicate Cu2+ ions starting to flow onto immobilized Aβ1–28 and when the flow 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

f6-ijms-13-11832: The sensorgram for the interactions between Cu2+ ions and Aβ1–42. Various concentrations (50, 100, 200, 300, and 400 μM, from top to bottom) of Cu2+ ions were injected onto the Aβ1–42 sensorchip. The inset shows the calibration curve for the interactions between various concentrations of Cu2+ with Aβ1–42. Each value represents the mean ± standard deviation of three separate injections. Arrows indicate Cu2+ ions starting to flow onto immobilized Aβ1–28 and when the flow of metal ions ends, respectively.
Mentions: Similar results were obtained for the Cu-Aβ1–42 interaction. As shown in Figure 6, the SPR angle shift increased with an increase of Cu2+ bound to the Aβ1–42-immobilized sensor chip. The calibration curve generated from the sensor exposed to different concentrations of Cu2+ is shown in the Figure 6 inset. A strong correlation coefficient (R2 = 0.99) was obtained for the linear regression equation calculated using Cu2+ concentrations ranging from 50 to 400 μM.

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